Target Binding Site Detail

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Target General Information
Ligand 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
Ligand General Information  Top
Ligand Name Methyl alpha-D-mannopyranoside Ligand Info
Canonical SMILES COC1C(C(C(C(O1)CO)O)O)O
InChI 1S/C7H14O6/c1-12-7-6(11)5(10)4(9)3(2-8)13-7/h3-11H,2H2,1H3/t3-,4-,5+,6+,7+/m1/s1
InChIKey HOVAGTYPODGVJG-VEIUFWFVSA-N
PubChem Compound ID 101798
Drug Binding Sites of Target  Top
PDB ID: 1KIU      FimH adhesin Q133N mutant-FimC chaperone complex with methyl-alpha-D-mannose
Method X-ray diffraction Resolution 3.00 Å Mutation Yes [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
LRNTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPTGG
160
CDVSARDVTV
170
TLPDYPGSVP
180
IPLTVYCAKS
190
QNLGYYLSGT
200

TADAGNSIFT
210
NTASFSPAQG
220
VGVQLTRNGT
230
IIPANNTVSL
240
GAVGTSAVSL
250

GLTANYARTG
260
GQVTAGNVQS
270
IIGVTFVYQ
Residue
Distance (Å)
PHE1
2.616
ILE13
3.312
HIS45
4.527
ASN46
3.147
ASP47
2.579
TYR48
3.443
ILE52
3.468
THR53
4.710
Residue
Distance (Å)
ASP54
2.591
ASN133
3.580
THR134
4.590
ASN135
3.190
ASN138
4.962
ASP140
4.548
PHE142
4.532
PDB ID: 5JCQ      Crystal structure of the FimH lectin domain from E.coli K12 in complex with methyl alpha-D-mannopyrannoside in spacegroup P21
Method X-ray diffraction Resolution 1.60 Å Mutation No [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
LRQTNNYNSD
140
DFQFVWNIYA
150

NNDVVVPT
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
PDB ID: 5JCR      Crystal structure of the FimH lectin domain from E.coli K12 in complex with methyl alpha-D-mannopyrannoside in spacegroup P212121
Method X-ray diffraction Resolution 1.70 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
Residue
Distance (Å)
PHE1
1.899
ILE13
2.629
GLY14
3.483
HIS45
4.171
ASN46
2.061
ASP47
1.934
TYR48
2.471
PRO49
4.851
ILE52
2.284
Residue
Distance (Å)
ASP54
2.077
GLN133
1.921
THR134
4.999
ASN135
1.895
TYR137
4.060
ASN138
3.444
ASP140
2.669
PHE142
2.745
PHE144
4.794
References  Top
REF 1 Structural basis of tropism of Escherichia coli to the bladder during urinary tract infection. Mol Microbiol. 2002 May;44(4):903-15.
REF 2 Crystal structure of the FimH lectin domain from E.coli K12 in complex with methyl alpha-D-mannopyrannoside in spacegroup P21
REF 3 Crystal structure of the FimH lectin domain from E.coli K12 in complex with methyl alpha-D-mannopyrannoside in spacegroup P212121

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