Binding Site Information of Target

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Target General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T46526 Target Info
Target Name Bacterial Fimbrin D-mannose adhesin (Bact FimH)
Synonyms fimH; b4320; Type 1 fimbrin D-mannose specific adhesin; Protein FimH; JW4283
Target Type Clinical trial Target
Gene Name Bact FimH
UniProt ID
FIMH_ECOLI
Drug Binding Sites of Target  Top
Ligand Name: Alpha-D-Mannose Ligand Info
Structure Description Co-crystals in the P212121 space group, of a beta-cyclodextrin spacered by triazole heptyl from alpha-D-mannose, with FimH lectin at 2.00 A resolution. PDB:6YHW
Method X-ray diffraction Resolution 1.96 Å Mutation No [1]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPTG
Residue
Distance (Å)
PHE1
1.880
ILE13
2.151
GLY14
3.170
HIS45
4.275
ASN46
2.264
ASP47
2.103
TYR48
2.282
PRO49
4.765
ILE52
2.432
THR53
4.874
Residue
Distance (Å)
ASP54
1.696
GLN133
2.215
THR134
4.311
ASN135
2.084
TYR137
4.855
ASN138
3.751
ASP140
2.276
PHE142
2.678
PHE144
4.783
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Edetic acid Ligand Info
Structure Description Breaking down the wall: mutation of the tyrosine gate of the universal Escherichia coli fimbrial adhesin FimH PDB:5FX3
Method X-ray diffraction Resolution 1.90 Å Mutation Yes [2]
PDB Sequence
FACTANGTAI
11
PIGGGSANVY
21
VNLAPVVNVG
31
QNLVVDLSTQ
41
IFCHNDYPET
51

ITDYVTLQRG
61
SAYGGVLSNF
71
SGTVKYSGSS
81
YPFPTTSETP
91
RVVYNSRTDK
101

PWPVALYLTP
111
VSSAGGVAIK
121
AGSLIAVLIL
131
RQTNNANSDD
141
FQFVWNIYAN
151

NDVVVPT
Residue
Distance (Å)
PRO49
3.684
GLU50
3.838
THR51
3.191
ILE52
3.395
Residue
Distance (Å)
THR53
2.029
ASN136
2.136
ALA137
3.429
Ligand Name: 2h-1,2,3-Triazol-4-Ylmethanol Ligand Info
Structure Description Co-crystals in the P212121 space group, of a beta-cyclodextrin spacered by triazole heptyl from alpha-D-mannose, with FimH lectin at 2.00 A resolution. PDB:6YHW
Method X-ray diffraction Resolution 1.96 Å Mutation No [1]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPTG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .TA5 or .TA52 or .TA53 or :3TA5;style chemicals stick;color identity;select .A:48 or .A:51 or .A:137; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TYR48
2.217
THR51
3.942
Residue
Distance (Å)
TYR137
3.532
Ligand Name: Heptane Ligand Info
Structure Description Co-crystals in the P212121 space group, of a beta-cyclodextrin spacered by triazole heptyl from alpha-D-mannose, with FimH lectin at 2.00 A resolution. PDB:6YHW
Method X-ray diffraction Resolution 1.96 Å Mutation No [1]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPTG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .HP6 or .HP62 or .HP63 or :3HP6;style chemicals stick;color identity;select .A:1 or .A:13 or .A:47 or .A:48 or .A:52 or .A:137; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
4.950
ILE13
3.943
ASP47
4.049
Residue
Distance (Å)
TYR48
2.493
ILE52
3.168
TYR137
3.025
Ligand Name: [2-[[(2~{s},3~{s},4~{s},5~{s},6~{r})-6-(Hydroxymethyl)-3,4,5-Tris(Oxidanyl)oxan-2-Yl]amino]-1,3-Thiazol-5-Yl]-(4-Methyl-2-Pyrazin-2-Yl-1,3-Thiazol-5-Yl)methanone Ligand Info
Structure Description Complex of FimH lectin with a TazMan (thiazolylaminomannosides) family member known as potent anti-adhesive agent at 2.6 A resolution PDB:5MTS
Method X-ray diffraction Resolution 2.60 Å Mutation No [3]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .XKA or .XKA2 or .XKA3 or :3XKA;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:51 or .A:52 or .A:54 or .A:133 or .A:134 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
2.813
ILE13
3.587
GLY14
4.571
HIS45
4.436
ASN46
3.299
ASP47
2.719
TYR48
3.158
THR51
4.411
ILE52
3.408
Residue
Distance (Å)
ASP54
2.292
GLN133
3.011
THR134
4.913
ASN135
3.083
TYR137
3.865
ASN138
4.880
ASP140
2.980
PHE142
3.435
Ligand Name: 4'-(Alpha-D-Mannopyranosyloxy)-Biphenyl-4-Methyl Sulfonamide Ligand Info
Structure Description Crystal structure of FimH in complex with a sulfonamide biphenyl alpha D-mannoside PDB:4CSS
Method X-ray diffraction Resolution 1.07 Å Mutation No [4]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVGGVAIKAG
123
SLIAVLILRQ
133
TNNYNSDDFQ
143
FVWNIYANND
153

VVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CWX or .CWX2 or .CWX3 or :3CWX;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:51 or .A:52 or .A:54 or .A:133 or .A:134 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
2.017
ILE13
2.732
GLY14
4.169
HIS45
4.550
ASN46
2.739
ASP47
2.049
TYR48
2.466
THR51
4.872
ILE52
2.187
Residue
Distance (Å)
ASP54
1.933
GLN133
2.064
THR134
4.781
ASN135
2.039
TYR137
3.513
ASN138
3.156
ASP140
2.739
PHE142
2.574
Ligand Name: 3'-Chloro-4'-(Alpha-D-Mannopyranosyloxy)biphenyl-4-Carbonitrile Ligand Info
Structure Description Crystal structure of FimH in complex with 3'-Chloro-4'-(alpha-D-mannopyranosyloxy)-biphenyl-4-carbonitrile PDB:4CST
Method X-ray diffraction Resolution 1.10 Å Mutation No [4]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPTG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CWK or .CWK2 or .CWK3 or :3CWK;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:49 or .A:52 or .A:53 or .A:54 or .A:133 or .A:134 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.923
ILE13
1.744
GLY14
4.059
HIS45
4.236
ASN46
1.993
ASP47
1.747
TYR48
2.345
PRO49
4.857
ILE52
2.378
Residue
Distance (Å)
THR53
4.694
ASP54
1.771
GLN133
1.814
THR134
4.765
ASN135
2.091
TYR137
3.227
ASN138
3.103
ASP140
2.681
PHE142
2.824
Ligand Name: 4-{[3-Chloro-4-(Alpha-D-Mannopyranosyloxy)phenyl]carbamoyl}benzoic Acid Ligand Info
Structure Description Crystal structure of FimH in complex with a benzoyl-amidophenyl alpha-D-mannopyranoside PDB:4X5P
Method X-ray diffraction Resolution 1.00 Å Mutation No [5]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .3XJ or .3XJ2 or .3XJ3 or :33XJ;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:49 or .A:52 or .A:53 or .A:54 or .A:98 or .A:133 or .A:134 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142 or .A:144; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.908
ILE13
2.469
GLY14
3.589
HIS45
4.506
ASN46
2.703
ASP47
2.054
TYR48
2.368
PRO49
4.873
ILE52
2.489
THR53
4.908
Residue
Distance (Å)
ASP54
1.636
ARG98
4.630
GLN133
2.178
THR134
4.282
ASN135
2.086
TYR137
3.194
ASN138
3.097
ASP140
1.747
PHE142
2.790
PHE144
4.994
Ligand Name: 4-(5-Nitro-1h-Indol-1-Yl)phenyl Alpha-D-Mannopyranoside Ligand Info
Structure Description Crystal structure of FimH in complex with 5-nitro-indolinylphenyl alpha-D-mannopyranoside PDB:4X5Q
Method X-ray diffraction Resolution 1.12 Å Mutation No [5]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .3XN or .3XN2 or .3XN3 or :33XN;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:49 or .A:51 or .A:52 or .A:53 or .A:54 or .A:133 or .A:134 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.906
ILE13
2.477
GLY14
3.674
HIS45
4.548
ASN46
2.738
ASP47
2.093
TYR48
2.391
PRO49
4.897
THR51
3.183
ILE52
2.439
Residue
Distance (Å)
THR53
4.767
ASP54
1.614
GLN133
2.133
THR134
4.222
ASN135
2.094
TYR137
2.585
ASN138
3.010
ASP140
1.734
PHE142
2.398
Ligand Name: 2-Chloro-4-{[2-(4-Methylpiperazin-1-Yl)-3,4-Dioxocyclobut-1-En-1-Yl]amino}phenyl Alpha-D-Mannopyranoside Ligand Info
Structure Description Crystal structure of FimH in complex with a squaryl-phenyl alpha-D-mannopyranoside derivative PDB:4X5R
Method X-ray diffraction Resolution 1.65 Å Mutation No [5]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .3XO or .3XO2 or .3XO3 or :33XO;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:49 or .A:50 or .A:52 or .A:54 or .A:98 or .A:133 or .A:134 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142 or .A:144; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.954
ILE13
2.299
GLY14
3.769
HIS45
4.313
ASN46
2.114
ASP47
2.050
TYR48
2.496
PRO49
4.897
GLU50
2.658
ILE52
2.276
Residue
Distance (Å)
ASP54
1.951
ARG98
3.296
GLN133
2.171
THR134
4.900
ASN135
2.003
TYR137
3.592
ASN138
3.554
ASP140
1.903
PHE142
2.166
PHE144
4.850
Ligand Name: Biphenyl-4-Yl Alpha-D-Mannopyranoside Ligand Info
Structure Description Crystal structure of FimH in complex with biphenyl alpha-D-mannopyranoside PDB:4X50
Method X-ray diffraction Resolution 2.00 Å Mutation No [5]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .3X8 or .3X82 or .3X83 or :33X8;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:51 or .A:52 or .A:54 or .A:133 or .A:134 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142 or .A:144; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.853
ILE13
2.590
GLY14
3.466
HIS45
4.650
ASN46
3.085
ASP47
1.858
TYR48
2.634
THR51
4.661
ILE52
2.412
Residue
Distance (Å)
ASP54
2.483
GLN133
1.854
THR134
4.785
ASN135
1.813
TYR137
2.359
ASN138
3.079
ASP140
2.681
PHE142
2.765
PHE144
4.717
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: 3-(4-methoxyphenyl)prop-2-yn-1-yl alpha-D-mannopyranoside Ligand Info
Structure Description FimH lectin domain co-crystal with a alpha-D-mannoside O-linked to a propynyl para methoxy phenyl PDB:4ATT
Method X-ray diffraction Resolution 1.25 Å Mutation No [6]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .HNV or .HNV2 or .HNV3 or :3HNV;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:52 or .A:54 or .A:133 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
2.783
ILE13
3.513
GLY14
4.867
HIS45
4.533
ASN46
3.125
ASP47
2.866
TYR48
3.499
ILE52
3.584
Residue
Distance (Å)
ASP54
2.544
GLN133
3.015
ASN135
2.841
TYR137
3.272
ASN138
4.975
ASP140
2.630
PHE142
3.916
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: N-{5-[(1r)-1-Hydroxyethyl]-1,3-Thiazol-2-Yl}-Alpha-D-Mannopyranosylamine Ligand Info
Structure Description A thiazolyl-mannoside bound to FimH, orthorhombic space group PDB:3ZL2
Method X-ray diffraction Resolution 1.25 Å Mutation No [7]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .BWG or .BWG2 or .BWG3 or :3BWG;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:52 or .A:54 or .A:133 or .A:134 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.958
ILE13
2.734
GLY14
4.065
HIS45
4.686
ASN46
2.797
ASP47
2.214
TYR48
3.150
ILE52
2.785
Residue
Distance (Å)
ASP54
2.435
GLN133
2.165
THR134
4.950
ASN135
2.071
TYR137
4.177
ASN138
4.439
ASP140
2.631
PHE142
2.771
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: (2r,3s,4s,5s,6s)-2-(Hydroxymethyl)-6-[3-(4-Phenylphenyl)prop-2-Ynoxy]oxane-3,4,5-Triol Ligand Info
Structure Description Structure of a triclinic crystal of the FimH lectin domain in complex with a propynyl biphenyl alpha-D-mannoside, at 1.4 A resolution PDB:4AV5
Method X-ray diffraction Resolution 1.40 Å Mutation No [8]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FYZ or .FYZ2 or .FYZ3 or :3FYZ;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:51 or .A:52 or .A:54 or .A:133 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.853
ILE13
2.620
GLY14
4.035
HIS45
4.692
ASN46
2.897
ASP47
2.127
TYR48
3.190
THR51
2.969
Residue
Distance (Å)
ILE52
2.626
ASP54
2.526
GLN133
2.100
ASN135
2.145
TYR137
3.131
ASN138
4.676
ASP140
2.690
PHE142
2.926
Ligand Name: Heptyl Alpha-D-Mannopyrannoside Ligand Info
Structure Description Breaking down the wall: mutation of the tyrosine gate of the universal Escherichia coli fimbrial adhesin FimH PDB:5FS5
Method X-ray diffraction Resolution 1.42 Å Mutation Yes [2]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNANSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .KGM or .KGM2 or .KGM3 or :3KGM;style chemicals stick;color identity;select .A:1 or .A:2 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:49 or .A:51 or .A:52 or .A:54 or .A:133 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.702
ALA2
4.898
ILE13
2.558
GLY14
4.123
HIS45
4.301
ASN46
2.054
ASP47
1.794
TYR48
2.336
PRO49
4.711
Residue
Distance (Å)
THR51
4.890
ILE52
2.183
ASP54
2.197
GLN133
1.792
ASN135
1.819
ALA137
4.141
ASN138
3.124
ASP140
2.658
PHE142
3.077
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: methyl 3-[3-chloranyl-4-[(2~{R},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-phenyl]benzoate Ligand Info
Structure Description Crystal structure of the lectin domain of the FimH variant Arg98Ala, in complex with Methyl 3-chloro-4-D-mannopyranosyloxy-3-biphenylcarboxylate PDB:7AYN
Method X-ray diffraction Resolution 1.42 Å Mutation Yes [9]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSATD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .SBQ or .SBQ2 or .SBQ3 or :3SBQ;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:49 or .A:52 or .A:54 or .A:133 or .A:134 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142 or .A:144; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.871
ILE13
2.407
GLY14
3.172
HIS45
4.402
ASN46
2.173
ASP47
2.085
TYR48
2.406
PRO49
3.352
ILE52
2.126
Residue
Distance (Å)
ASP54
1.824
GLN133
2.168
THR134
4.994
ASN135
1.904
TYR137
3.288
ASN138
3.213
ASP140
1.890
PHE142
2.865
PHE144
4.845
Ligand Name: D-Mannose Alpha1o P-Hydroxypropynyl-Phenyl Ligand Info
Structure Description FimH lectin domain co-crystal with a alpha-D-mannoside O-linked to para hydroxypropargyl phenyl PDB:4AUJ
Method X-ray diffraction Resolution 1.53 Å Mutation No [6]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .HNW or .HNW2 or .HNW3 or :3HNW;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:52 or .A:54 or .A:133 or .A:134 or .A:135 or .A:137 or .A:140 or .A:142; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
2.741
ILE13
3.545
GLY14
4.703
HIS45
4.659
ASN46
3.054
ASP47
2.835
TYR48
3.388
ILE52
3.608
Residue
Distance (Å)
ASP54
2.523
GLN133
3.012
THR134
4.941
ASN135
2.842
TYR137
4.246
ASP140
2.690
PHE142
3.655
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: (6r)-1,6-Anhydro-2-O-Heptyl-6-(Hydroxymethyl)-D-Galactitol Ligand Info
Structure Description Crystal structure of FimH in complex with heptyl alpha-D-septanoside PDB:5CGB
Method X-ray diffraction Resolution 1.60 Å Mutation No [10]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .51C or .51C2 or .51C3 or :351C;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:49 or .A:51 or .A:52 or .A:54 or .A:133 or .A:134 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142 or .A:144; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.997
ILE13
2.147
GLY14
3.230
HIS45
4.563
ASN46
2.785
ASP47
2.071
TYR48
2.099
PRO49
4.800
THR51
4.775
ILE52
2.425
Residue
Distance (Å)
ASP54
1.779
GLN133
2.115
THR134
4.327
ASN135
2.089
TYR137
2.782
ASN138
2.719
ASP140
2.238
PHE142
2.842
PHE144
4.891
Ligand Name: Methyl alpha-D-mannopyranoside Ligand Info
Structure Description Crystal structure of the FimH lectin domain from E.coli K12 in complex with methyl alpha-D-mannopyrannoside in spacegroup P21 PDB:5JCQ
Method X-ray diffraction Resolution 1.60 Å Mutation No [11]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .MMA or .MMA2 or .MMA3 or :3MMA;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:49 or .A:52 or .A:54 or .A:133 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142 or .A:144; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.935
ILE13
2.658
GLY14
3.487
HIS45
4.245
ASN46
2.000
ASP47
2.001
TYR48
2.436
PRO49
4.846
ILE52
2.186
Residue
Distance (Å)
ASP54
2.072
GLN133
1.803
ASN135
1.890
TYR137
4.044
ASN138
3.491
ASP140
2.672
PHE142
2.788
PHE144
4.795
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: 5-[4-[(2~{r},3~{s},4~{s},5~{s},6~{r})-6-(Hydroxymethyl)-3,4,5-Tris(Oxidanyl)oxan-2-Yl]oxy-3-Methyl-Phenyl]-~{n}1,~{n}3-Dimethyl-Benzene-1,3-Dicarboxamide Ligand Info
Structure Description Crystal structure of para-biphenyl-2-methyl-3', 5' di-methyl amide mannoside bound to FimH lectin domain PDB:5F2F
Method X-ray diffraction Resolution 1.67 Å Mutation No [12]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .5U7 or .5U72 or .5U73 or :35U7;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:49 or .A:50 or .A:52 or .A:53 or .A:54 or .A:98 or .A:133 or .A:134 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.902
ILE13
1.977
GLY14
4.125
HIS45
4.490
ASN46
2.865
ASP47
1.955
TYR48
2.555
PRO49
4.860
GLU50
3.499
ILE52
2.295
Residue
Distance (Å)
THR53
4.824
ASP54
1.903
ARG98
2.039
GLN133
2.155
THR134
4.767
ASN135
2.056
TYR137
2.770
ASN138
2.795
ASP140
2.719
PHE142
2.537
Ligand Name: Butyl alpha-D-mannopyranoside Ligand Info
Structure Description 1.7 A resolution structure of the receptor binding domain of the FimH adhesin from uropathogenic E. coli PDB:1UWF
Method X-ray diffraction Resolution 1.69 Å Mutation No [13]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .DEG or .DEG2 or .DEG3 or :3DEG;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:52 or .A:54 or .A:133 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
2.766
ILE13
3.465
GLY14
4.655
HIS45
4.639
ASN46
3.063
ASP47
2.904
TYR48
3.659
ILE52
3.588
Residue
Distance (Å)
ASP54
2.479
GLN133
3.098
ASN135
2.911
TYR137
3.663
ASN138
4.873
ASP140
2.589
PHE142
3.650
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: 3-[4-[(2~{r},3~{s},4~{s},5~{s},6~{r})-6-(Hydroxymethyl)-3,4,5-Tris(Oxidanyl)oxan-2-Yl]oxy-3-Methyl-Phenyl]-~{n}-Methyl-Benzamide Ligand Info
Structure Description Crystal structure of para-biphenyl-2-methyl-3'-methyl amide mannoside bound to FimH lectin domain PDB:5F3F
Method X-ray diffraction Resolution 1.76 Å Mutation No [14]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .5US or .5US2 or .5US3 or :35US;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:49 or .A:50 or .A:52 or .A:54 or .A:98 or .A:133 or .A:134 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142 or .A:144; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.987
ILE13
2.533
GLY14
3.480
HIS45
4.114
ASN46
2.085
ASP47
2.000
TYR48
2.518
PRO49
4.705
GLU50
3.535
ILE52
1.968
Residue
Distance (Å)
ASP54
1.868
ARG98
2.221
GLN133
1.945
THR134
4.816
ASN135
2.097
TYR137
2.746
ASN138
2.751
ASP140
2.754
PHE142
2.716
PHE144
4.890
Ligand Name: 3-Fluoro-Heptylmannoside Ligand Info
Structure Description Crystal structure of FimH lectin domain in complex with 3-Fluoro-Heptylmannoside PDB:5L4W
Method X-ray diffraction Resolution 1.90 Å Mutation No [15]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .6KH or .6KH2 or .6KH3 or :36KH;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:52 or .A:54 or .A:133 or .A:134 or .A:135 or .A:137 or .A:140 or .A:142; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
2.718
ILE13
3.513
GLY14
4.620
HIS45
4.712
ASN46
3.215
ASP47
2.918
TYR48
3.601
ILE52
3.655
Residue
Distance (Å)
ASP54
2.514
GLN133
3.018
THR134
4.913
ASN135
2.891
TYR137
3.550
ASP140
3.247
PHE142
3.375
Ligand Name: 3-Pyridin-3-Ylprop-2-Yn-1-Yl Alpha-D-Mannopyranoside Ligand Info
Structure Description FimH lectin domain co-crystal with a alpha-D-mannoside O-linked to a propynyl pyridine PDB:4AV4
Method X-ray diffraction Resolution 1.90 Å Mutation No [8]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVNLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FVQ or .FVQ2 or .FVQ3 or :3FVQ;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:51 or .A:52 or .A:54 or .A:133 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.760
ILE13
2.663
GLY14
3.901
HIS45
4.544
ASN46
2.643
ASP47
1.934
TYR48
2.941
THR51
4.969
Residue
Distance (Å)
ILE52
2.499
ASP54
2.534
GLN133
2.334
ASN135
1.898
TYR137
2.365
ASN138
4.429
ASP140
2.517
PHE142
2.807
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: 4-Deoxy-Heptylmannoside Ligand Info
Structure Description Crystal structure of FimH lectin domain in complex with 4-Deoxy-Heptylmannoside PDB:5L4X
Method X-ray diffraction Resolution 1.90 Å Mutation No [16]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .6KU or .6KU2 or .6KU3 or :36KU;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:49 or .A:51 or .A:52 or .A:54 or .A:133 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.842
ILE13
1.961
GLY14
3.764
HIS45
4.582
ASN46
2.875
ASP47
2.087
TYR48
2.353
PRO49
4.857
THR51
4.488
Residue
Distance (Å)
ILE52
2.479
ASP54
2.011
GLN133
1.638
ASN135
2.507
TYR137
2.836
ASN138
3.466
ASP140
2.553
PHE142
2.968
Ligand Name: 4-Fluoro-Heptylmannoside Ligand Info
Structure Description Crystal structure of FimH lectin domain in complex with 4-Fluoro-Heptylmannoside PDB:5L4Y
Method X-ray diffraction Resolution 1.90 Å Mutation No [17]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .6K3 or .6K32 or .6K33 or :36K3;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:52 or .A:54 or .A:133 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
2.702
ILE13
3.682
GLY14
4.835
HIS45
4.602
ASN46
3.165
ASP47
2.862
TYR48
3.611
ILE52
3.340
Residue
Distance (Å)
ASP54
2.623
GLN133
2.995
ASN135
2.971
TYR137
3.424
ASN138
4.720
ASP140
2.704
PHE142
3.867
Ligand Name: heptyl 2-deoxy-alpha-D-mannopyranoside Ligand Info
Structure Description Crystal structure of FimH lectin domain in complex with 2-Deoxy-Heptylmannoside PDB:5L4T
Method X-ray diffraction Resolution 1.90 Å Mutation No [18]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .6LS or .6LS2 or .6LS3 or :36LS;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:49 or .A:52 or .A:54 or .A:133 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.930
ILE13
2.499
GLY14
4.114
HIS45
4.406
ASN46
2.321
ASP47
2.094
TYR48
2.410
PRO49
4.928
Residue
Distance (Å)
ILE52
2.146
ASP54
1.784
GLN133
2.137
ASN135
2.029
TYR137
2.964
ASN138
3.527
ASP140
2.813
PHE142
2.304
Ligand Name: N6-Acetyl-L-lysine Ligand Info
Structure Description Breaking down the wall: mutation of the tyrosine gate of the universal Escherichia coli fimbrial adhesin FimH PDB:5FX3
Method X-ray diffraction Resolution 1.90 Å Mutation Yes [2]
PDB Sequence
FACTANGTAI
11
PIGGGSANVY
21
VNLAPVVNVG
31
QNLVVDLSTQ
41
IFCHNDYPET
51

ITDYVTLQRG
61
SAYGGVLSNF
71
SGTVKYSGSS
81
YPFPTTSETP
91
RVVYNSRTDK
101

PWPVALYLTP
111
VSSAGGVAIK
121
AGSLIAVLIL
131
RQTNNANSDD
141
FQFVWNIYAN
151

NDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ALY or .ALY2 or .ALY3 or :3ALY;style chemicals stick;color identity;select .A:2 or .A:3 or .A:5 or .A:6 or .A:8 or .A:9 or .A:10 or .A:11 or .A:41 or .A:42 or .A:43 or .A:44 or .A:45 or .A:100 or .A:146; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA2
4.616
CYS3
1.319
THR5
1.331
ALA6
3.721
GLY8
3.298
THR9
2.244
ALA10
2.210
ILE11
3.285
Residue
Distance (Å)
GLN41
3.927
ILE42
2.787
PHE43
2.094
CYS44
4.212
HIS45
4.740
ASP100
2.243
TRP146
3.425
Ligand Name: 2-Fluoro-Heptylmannoside Ligand Info
Structure Description Crystal structure of FimH lectin domain in complex with 2-Fluoro-Heptylmannoside PDB:5L4U
Method X-ray diffraction Resolution 2.10 Å Mutation No [19]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .6KS or .6KS2 or .6KS3 or :36KS;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:52 or .A:54 or .A:133 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
2.734
ILE13
3.455
GLY14
4.866
HIS45
4.582
ASN46
3.105
ASP47
2.807
TYR48
3.591
ILE52
3.340
Residue
Distance (Å)
ASP54
2.581
GLN133
3.090
ASN135
2.943
TYR137
3.498
ASN138
4.609
ASP140
2.683
PHE142
3.824
Ligand Name: 4-[3-chloranyl-4-[(2~{R},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-phenyl]-2,3,5,6-tetrakis(fluoranyl)benzenecarbonitrile Ligand Info
Structure Description Crystal structure of FimH in complex with a tetraflourinated biphenyl alpha D-mannoside PDB:6G2R
Method X-ray diffraction Resolution 2.10 Å Mutation No [20]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .EJK or .EJK2 or .EJK3 or :3EJK;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:49 or .A:51 or .A:52 or .A:54 or .A:133 or .A:134 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.845
ILE13
1.881
GLY14
3.888
HIS45
4.165
ASN46
2.156
ASP47
1.801
TYR48
2.442
PRO49
4.910
THR51
4.665
Residue
Distance (Å)
ILE52
2.586
ASP54
2.070
GLN133
1.741
THR134
4.073
ASN135
1.836
TYR137
2.858
ASN138
3.293
ASP140
2.730
PHE142
2.862
Ligand Name: Methanol Triazol Ethyl Phenyl 1o-Alpha-D-Mannopyranoside Ligand Info
Structure Description Structure of the FimH lectin domain in the trigonal space group, in complex with a methanol triazol ethyl phenyl alpha-D-mannoside at 2.1 A resolution PDB:4AVJ
Method X-ray diffraction Resolution 2.10 Å Mutation No [8]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .J73 or .J732 or .J733 or :3J73;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:51 or .A:52 or .A:54 or .A:133 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.892
ILE13
2.663
GLY14
4.060
HIS45
4.693
ASN46
2.938
ASP47
2.085
TYR48
2.509
THR51
3.352
Residue
Distance (Å)
ILE52
3.014
ASP54
2.495
GLN133
2.293
ASN135
2.128
TYR137
3.220
ASN138
4.065
ASP140
2.536
PHE142
3.012
Ligand Name: Propyl Thiopropyl Alpha-D-Mannopyranoside Ligand Info
Structure Description Structure of the FimH lectin domain in the trigonal space group, in complex with a thioalkyl alpha-D-mannoside at 2.1 A resolution PDB:4AVH
Method X-ray diffraction Resolution 2.10 Å Mutation No [8]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FK9 or .FK92 or .FK93 or :3FK9;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:51 or .A:52 or .A:54 or .A:133 or .A:134 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
2.734
ILE13
3.604
GLY14
4.636
HIS45
4.847
ASN46
3.231
ASP47
2.889
TYR48
3.374
THR51
3.869
ILE52
3.747
Residue
Distance (Å)
ASP54
2.592
GLN133
3.003
THR134
4.977
ASN135
2.743
TYR137
3.709
ASN138
4.996
ASP140
2.806
PHE142
3.608
Ligand Name: (2~{R},3~{S},4~{S},5~{S},6~{R})-2-(hydroxymethyl)-6-[4-[2,3,4,5,6-pentakis(fluoranyl)phenyl]phenoxy]oxane-3,4,5-triol Ligand Info
Structure Description Crystal structure of FimH in complex with a pentaflourinated biphenyl alpha D-mannoside PDB:6G2S
Method X-ray diffraction Resolution 2.20 Å Mutation No [20]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .EJN or .EJN2 or .EJN3 or :3EJN;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:51 or .A:52 or .A:54 or .A:133 or .A:134 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142 or .A:144; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.789
ILE13
2.430
GLY14
3.352
HIS45
4.403
ASN46
2.452
ASP47
2.127
TYR48
2.495
THR51
3.236
ILE52
2.447
Residue
Distance (Å)
ASP54
1.960
GLN133
2.337
THR134
4.179
ASN135
2.327
TYR137
2.524
ASN138
3.611
ASP140
2.023
PHE142
2.942
PHE144
4.807
Ligand Name: (2r,3s,4r,5s,6r)-2-(Hydroxymethyl)-6-[3-(Naphthalen-1-Yl)propyl]oxane-3,4,5-Triol Ligand Info
Structure Description Complex of the FimH lectin with a C-linked naphtyl alpha-D-mannoside in soaked trigonal crystals at 2.40 A resolution PDB:5ABZ
Method X-ray diffraction Resolution 2.40 Å Mutation No [21]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .Z47 or .Z472 or .Z473 or :3Z47;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:49 or .A:51 or .A:52 or .A:54 or .A:133 or .A:134 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142 or .A:144; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.733
ILE13
2.250
GLY14
3.278
HIS45
4.376
ASN46
2.848
ASP47
1.633
TYR48
2.364
PRO49
4.961
THR51
3.372
ILE52
2.458
Residue
Distance (Å)
ASP54
2.250
GLN133
2.011
THR134
4.127
ASN135
1.976
TYR137
2.569
ASN138
3.640
ASP140
1.853
PHE142
2.676
PHE144
4.840
Ligand Name: Methyl Ester Octyl Alpha-1o-D-Mannopyrannoside Ligand Info
Structure Description Structure of the FimH lectin domain in the trigonal space group, in complex with a methyl ester octyl alpha-D-mannoside at 2.4 A resolution PDB:4AVI
Method X-ray diffraction Resolution 2.40 Å Mutation No [8]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .XNS or .XNS2 or .XNS3 or :3XNS;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:51 or .A:52 or .A:54 or .A:133 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
1.769
ILE13
2.946
GLY14
4.174
HIS45
4.751
ASN46
2.976
ASP47
2.289
TYR48
2.974
THR51
2.731
Residue
Distance (Å)
ILE52
2.841
ASP54
2.516
GLN133
2.351
ASN135
2.187
TYR137
2.416
ASN138
4.331
ASP140
2.730
PHE142
2.916
Ligand Name: 1,5-Anhydro-d-mannitol Ligand Info
Structure Description Crystal structure of the FimH lectin domain in complex with 1,5-Anhydromannitol PDB:5MUC
Method X-ray diffraction Resolution 2.60 Å Mutation No [22]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .AH2 or .AH22 or .AH23 or :3AH2;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:49 or .A:52 or .A:54 or .A:133 or .A:134 or .A:135 or .A:137 or .A:138 or .A:140 or .A:142; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
2.024
ILE13
2.336
GLY14
3.594
HIS45
4.305
ASN46
2.219
ASP47
2.009
TYR48
2.127
PRO49
4.689
ILE52
2.470
Residue
Distance (Å)
ASP54
1.670
GLN133
2.208
THR134
4.158
ASN135
2.193
TYR137
4.878
ASN138
3.326
ASP140
2.093
PHE142
2.813
Ligand Name: 3-Deoxy-Heptylmannoside Ligand Info
Structure Description Crystal structure of FimH lectin domain in complex with 3-Deoxy-Heptylmannoside PDB:5L4V
Method X-ray diffraction Resolution 2.99 Å Mutation No [23]
PDB Sequence
FACKTANGTA
10
IPIGGGSANV
20
YVNLAPVVNV
30
GQNLVVDLST
40
QIFCHNDYPE
50

TITDYVTLQR
60
GSAYGGVLSN
70
FSGTVKYSGS
80
SYPFPTTSET
90
PRVVYNSRTD
100

KPWPVALYLT
110
PVSSAGGVAI
120
KAGSLIAVLI
130
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .6KW or .6KW2 or .6KW3 or :36KW;style chemicals stick;color identity;select .A:1 or .A:13 or .A:14 or .A:45 or .A:46 or .A:47 or .A:48 or .A:52 or .A:54 or .A:133 or .A:134 or .A:135 or .A:137 or .A:140 or .A:142; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE1
2.727
ILE13
3.483
GLY14
4.630
HIS45
4.730
ASN46
3.211
ASP47
2.912
TYR48
3.615
ILE52
3.652
Residue
Distance (Å)
ASP54
2.545
GLN133
3.339
THR134
4.938
ASN135
2.865
TYR137
3.543
ASP140
3.312
PHE142
4.390
References  Top
REF 1 The Antiadhesive Strategy in Crohn's Disease: Orally Active Mannosides to Decolonize Pathogenic Escherichia coli from the Gut. Chembiochem. 2016 May 17;17(10):936-52.
REF 2 Mutation of Tyr137 of the universal Escherichia coli fimbrial adhesin FimH relaxes the tyrosine gate prior to mannose binding. IUCrJ. 2017 Jan 1;4(Pt 1):7-23.
REF 3 Physiochemical Tuning of Potent Escherichia coli Anti-Adhesives by Microencapsulation and Methylene Homologation. ChemMedChem. 2017 Jun 21;12(12):986-998.
REF 4 FimH antagonists: bioisosteres to improve the in vitro and in vivo PK/PD profile. J Med Chem. 2015 Mar 12;58(5):2221-39.
REF 5 The tyrosine gate of the bacterial lectin FimH: a conformational analysis by NMR spectroscopy and X-ray crystallography. Chembiochem. 2015 May 26;16(8):1235-46.
REF 6 Validation of Reactivity Descriptors to Assess the Aromatic Stacking within the Tyrosine Gate of FimH. ACS Med Chem Lett. 2013 Sep 13;4(11):1085-90.
REF 7 Thiazolylaminomannosides as potent antiadhesives of type 1 piliated Escherichia coli isolated from Crohn's disease patients. J Med Chem. 2013 Jul 11;56(13):5395-406.
REF 8 The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry. 2012 Jun 19;51(24):4790-9.
REF 9 Does targeting Arg98 of FimH lead to high affinity antagonists?. Eur J Med Chem. 2021 Feb 5;211:113093.
REF 10 The price of flexibility - a case study on septanoses as pyranose mimetics. Chem Sci. 2017 Nov 8;9(3):646-654.
REF 11 Crystal structure of the FimH lectin domain from E.coli K12 in complex with methyl alpha-D-mannopyrannoside in spacegroup P21
REF 12 Antivirulence Isoquinolone Mannosides: Optimization of the Biaryl Aglycone for FimH Lectin Binding Affinity and Efficacy in the Treatment of Chronic UTI. ChemMedChem. 2016 Feb 17;11(4):367-73.
REF 13 Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin. Mol Microbiol. 2005 Jan;55(2):441-55.
REF 14 Crystal structure of para-biphenyl-2-methyl-3'-methyl amide mannoside bound to FimH lectin domain
REF 15 Crystal structure of FimH lectin domain in complex with 3-Fluoro-Heptylmannoside
REF 16 Crystal structure of FimH lectin domain in complex with 4-Deoxy-Heptylmannoside
REF 17 Crystal structure of FimH lectin domain in complex with 4-Fluoro-Heptylmannoside
REF 18 Crystal structure of FimH lectin domain in complex with 2-Deoxy-Heptylmannoside
REF 19 Crystal structure of FimH lectin domain in complex with 2-Fluoro-Heptylmannoside
REF 20 Improvement of Aglycone Pi-Stacking Yields Nanomolar to Sub-nanomolar FimH Antagonists. ChemMedChem. 2019 Apr 3;14(7):749-757.
REF 21 Structures of C-mannosylated anti-adhesives bound to the type 1 fimbrial FimH adhesin. IUCrJ. 2016 Feb 26;3(Pt 3):163-7.
REF 22 KinITC-One Method Supports both Thermodynamic and Kinetic SARs as Exemplified on FimH Antagonists. Chemistry. 2018 Sep 3;24(49):13049-13057.
REF 23 Crystal structure of FimH lectin domain in complex with 3-Deoxy-Heptylmannoside

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