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 T09544 Target Info
Target Name Galectin-1 (LGALS1)
Synonyms SLac lectin 1; S-Lac lectin 1; Putative MAPKactivating protein PM12; Putative MAPK-activating protein PM12; Lectin galactosidebinding soluble 1; Lectin galactoside-binding soluble 1; Lactosebinding lectin 1; Lactose-binding lectin 1; HPL; HLBP14; HBL; Galaptin; Gal1; Gal-1; Betagalactosidebinding lectin L14I; Beta-galactoside-binding lectin L-14-I; 14 kDa lectin; 14 kDa lamininbinding protein; 14 kDa laminin-binding protein
Target Type Patented-recorded Target
Gene Name LGALS1
UniProt ID
LEG1_HUMAN
Ligand General Information  Top
Ligand Name S,S-(2-Hydroxyethyl)Thiocysteine Ligand Info
Canonical SMILES C(CSSCC(C(=O)O)N)O
InChI 1S/C5H11NO3S2/c6-4(5(8)9)3-11-10-2-1-7/h4,7H,1-3,6H2,(H,8,9)/t4-/m0/s1
InChIKey YPUBRSXDQSFQBA-BYPYZUCNSA-N
PubChem Compound ID 170018
Drug Binding Sites of Target  Top
PDB ID: 3T2T      Crystal structure of human galectin-1 in complex with methyl 2-O-acetyl-3-O-toluoyl-beta-D-talopyranoside
Method X-ray diffraction Resolution 1.90 Å Mutation No [1]
PDB Sequence
ACGLVASNLN
10
LKPGELRVRG
21
EVAPDAKSFV
31
LNLGKDSNNL
41
CLHFNPRFNA
51

HGDANTIVCN
61
SKDGGAWGTE
71
QREAVFPFQP
81
GSVAEVITFD
92
QANLTVKLPD
102

GYEFKFPNRL
112
NLEAINYMAA
122
DGDFKIKVAF
133
D
Residue
Distance (Å)
LEU11
4.121
GLY14
3.985
GLU15
1.323
LEU17
1.332
ARG18
3.633
VAL19
3.508
ARG20
2.903
GLU86
3.062
VAL87
1.336
ILE89
1.329
THR90
3.929
THR97
3.823
Residue
Distance (Å)
VAL98
3.545
LYS99
2.832
LEU100
2.981
PRO101
3.299
ASP102
4.946
ILE128
3.759
LYS129
1.341
VAL131
1.320
ALA132
3.690
PHE133
3.454
ASP134
2.761
PDB ID: 4Q2F      Galectin-1 in Complex with Ligand AN020
Method X-ray diffraction Resolution 1.40 Å Mutation No [2]
PDB Sequence
CGLVASNLNL
11
KPGELRVRGE
22
VAPDAKSFVL
32
NLGKDSNNLC
42
LHFNPRFNAH
52

GDANTIVCNS
62
KDGGAWGTEQ
72
REAVFPFQPG
82
SVAEVITFDQ
93
ANLTVKLPDG
103

YEFKFPNRLN
113
LEAINYMAAD
123
GDFKIKVAFD
134
Residue
Distance (Å)
LEU11
3.229
GLY14
3.995
GLU15
1.336
LEU17
1.329
ARG18
2.358
VAL19
2.553
ARG20
1.970
GLU86
2.419
VAL87
1.331
ILE89
1.325
THR90
1.988
THR97
3.696
Residue
Distance (Å)
VAL98
2.795
LYS99
1.913
LEU100
3.136
PRO101
2.642
ASP102
4.910
ILE128
3.169
LYS129
1.335
VAL131
1.332
ALA132
3.279
PHE133
3.067
ASP134
1.859
PDB ID: 4Q1P      Galectin-1 in Complex with Ligand NB169
Method X-ray diffraction Resolution 1.46 Å Mutation No [3]
PDB Sequence
CGLVASNLNL
11
KPGELRVRGE
22
VAPDAKSFVL
32
NLGKDSNNLC
42
LHFNPRFNAH
52

GDANTIVCNS
62
KDGGAWGTEQ
72
REAVFPFQPG
82
SVAEVITFDQ
93
ANLTVKLPDG
103

YEFKFPNRLN
113
LEAINYMAAD
123
GDFKIKVAFD
134
Residue
Distance (Å)
LEU11
3.240
GLY14
4.024
GLU15
1.331
LEU17
1.327
ARG18
2.585
VAL19
2.631
ARG20
1.996
GLU86
2.528
VAL87
1.324
ILE89
1.327
THR90
2.137
Residue
Distance (Å)
THR97
3.744
VAL98
2.809
LYS99
1.902
LEU100
3.300
PRO101
2.764
ILE128
3.235
LYS129
1.323
VAL131
1.330
ALA132
3.224
PHE133
3.078
ASP134
2.024
PDB ID: 4Q1R      Galectin-1 in Complex with Ligand AN027
Method X-ray diffraction Resolution 1.47 Å Mutation No [4]
PDB Sequence
CGLVASNLNL
11
KPGELRVRGE
22
VAPDAKSFVL
32
NLGKDSNNLC
42
LHFNPRFNAH
52

GDANTIVCNS
62
KDGGAWGTEQ
72
REAVFPFQPG
82
SVAEVITFDQ
93
ANLTVKLPDG
103

YEFKFPNRLN
113
LEAINYMAAD
123
GDFKIKVAFD
134
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CME or .CME2 or .CME3 or :3CME;style chemicals stick;color identity;select .A:11 or .A:14 or .A:15 or .A:17 or .A:18 or .A:19 or .A:20 or .A:86 or .A:87 or .A:89 or .A:90 or .A:97 or .A:98 or .A:99 or .A:100 or .A:101 or .A:102 or .A:128 or .A:129 or .A:131 or .A:132 or .A:133 or .A:134; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU11
3.273
GLY14
3.922
GLU15
1.331
LEU17
1.330
ARG18
2.574
VAL19
2.618
ARG20
2.053
GLU86
2.556
VAL87
1.329
ILE89
1.326
THR90
2.098
THR97
3.711
Residue
Distance (Å)
VAL98
2.777
LYS99
1.897
LEU100
3.420
PRO101
2.672
ASP102
4.865
ILE128
3.234
LYS129
1.325
VAL131
1.331
ALA132
3.231
PHE133
3.024
ASP134
2.320
PDB ID: 6F83      Crystal Structure of Human Galectin-1 in Complex With Thienyl-1,2, 3-triazolyl Thiodigalactoside Inhibitor
Method X-ray diffraction Resolution 2.20 Å Mutation No [5]
PDB Sequence
ACGLVASNLN
10
LKPGELRVRG
21
EVAPDAKSFV
31
LNLGKDSNNL
41
LHFNPRFNAH
52

GDANTIVNSK
63
DGGAWGTEQR
73
EAVFPFQPGS
83
VAEVITFDQA
94
NLTVKLPDGY
104

EFKFPNRLNL
114
EAINYMAADG
124
DFKIKVAFD
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CME or .CME2 or .CME3 or :3CME;style chemicals stick;color identity;select .A:11 or .A:14 or .A:15 or .A:17 or .A:18 or .A:19 or .A:20 or .A:34 or .A:35 or .A:40 or .A:41 or .A:43 or .A:44 or .A:45 or .A:58 or .A:59 or .A:61 or .A:62 or .A:70 or .A:71 or .A:72 or .A:73 or .A:74 or .A:86 or .A:87 or .A:89 or .A:90 or .A:91 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:101 or .A:106 or .A:107 or .A:108 or .A:109 or .A:110 or .A:112 or .A:113 or .A:114 or .A:116 or .A:117 or .A:128 or .A:129 or .A:131 or .A:132 or .A:133 or .A:134; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU11
4.406
GLY14
4.076
GLU15
1.330
LEU17
1.322
ARG18
3.365
VAL19
3.534
ARG20
2.846
LEU34
2.778
GLY35
3.873
ASN40
4.140
LEU41
1.325
LEU43
1.327
HIS44
3.136
PHE45
3.920
ILE58
3.892
VAL59
1.332
ASN61
1.319
SER62
4.383
THR70
4.441
GLU71
3.563
GLN72
2.852
ARG73
4.274
GLU74
2.757
GLU86
3.498
VAL87
1.329
Residue
Distance (Å)
ILE89
1.332
THR90
3.313
PHE91
3.786
LEU96
3.439
THR97
3.743
VAL98
3.334
LYS99
2.750
LEU100
2.888
PRO101
3.785
PHE106
3.100
LYS107
3.551
PHE108
3.705
PRO109
4.731
ASN110
2.451
LEU112
3.721
ASN113
3.397
LEU114
3.195
ALA116
4.544
ILE117
3.485
ILE128
3.508
LYS129
1.333
VAL131
1.327
ALA132
3.686
PHE133
3.511
ASP134
2.976
PDB ID: 5MWX      Galectin-1 in Complex with Ligand JB60
Method X-ray diffraction Resolution 1.29 Å Mutation No [6]
PDB Sequence
CGLVASNLNL
11
KPGELRVRGE
22
VAPDAKSFVL
32
NLGKDSNNLC
42
LHFNPRFNAH
52

GDANTIVCNS
62
KDGGAWGTEQ
72
REAVFPFQPG
82
SVAEVITFDQ
93
ANLTVKLPDG
103

YEFKFPNRLN
113
LEAINYMAAD
123
GDFKIKVAFD
134
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CME or .CME2 or .CME3 or :3CME;style chemicals stick;color identity;select .A:11 or .A:14 or .A:15 or .A:17 or .A:18 or .A:19 or .A:20 or .A:21 or .A:86 or .A:87 or .A:89 or .A:90 or .A:97 or .A:98 or .A:99 or .A:100 or .A:101 or .A:102 or .A:128 or .A:129 or .A:131 or .A:132 or .A:133 or .A:134; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU11
3.140
GLY14
3.996
GLU15
1.334
LEU17
1.332
ARG18
2.465
VAL19
2.665
ARG20
2.022
GLY21
4.423
GLU86
2.407
VAL87
1.318
ILE89
1.316
THR90
2.176
Residue
Distance (Å)
THR97
3.635
VAL98
2.787
LYS99
1.853
LEU100
3.182
PRO101
2.584
ASP102
4.837
ILE128
2.939
LYS129
1.314
VAL131
1.343
ALA132
3.324
PHE133
3.125
ASP134
1.986
PDB ID: 7NML      Galectin-1 in complex with 4-Amino-6-chloro-1,3-benzenedisulfonamide
Method X-ray diffraction Resolution 1.43 Å Mutation No [7]
PDB Sequence
CGLVASNLNL
11
KPGELRVRGE
22
VAPDAKSFVL
32
NLGKDSNNLC
42
LHFNPRFNAH
52

GDANTIVCNS
62
KDGGAWGTEQ
72
REAVFPFQPG
82
SVAEVITFDQ
93
ANLTVKLPDG
103

YEFKFPNRLN
113
LEAINYMAAD
123
GDFKIKVAFD
134
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CME or .CME2 or .CME3 or :3CME;style chemicals stick;color identity;select .A:11 or .A:14 or .A:15 or .A:17 or .A:18 or .A:19 or .A:20 or .A:21 or .A:86 or .A:87 or .A:89 or .A:90 or .A:97 or .A:98 or .A:99 or .A:100 or .A:101 or .A:102 or .A:103 or .A:128 or .A:129 or .A:131 or .A:132 or .A:133 or .A:134; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU11
3.167
GLY14
3.975
GLU15
1.328
LEU17
1.321
ARG18
2.082
VAL19
2.655
ARG20
2.037
GLY21
4.957
GLU86
2.187
VAL87
1.333
ILE89
1.333
THR90
2.247
THR97
3.578
Residue
Distance (Å)
VAL98
2.710
LYS99
1.905
LEU100
3.045
PRO101
2.759
ASP102
4.596
GLY103
4.895
ILE128
3.312
LYS129
1.317
VAL131
1.347
ALA132
2.519
PHE133
3.043
ASP134
2.402
PDB ID: 5MWT      Galectin-1 in Complex with Ligand JB97
Method X-ray diffraction Resolution 1.71 Å Mutation No [8]
PDB Sequence
CGLVASNLNL
11
KPGELRVRGE
22
VAPDAKSFVL
32
NLGKDSNNLC
42
LHFNPRFNAH
52

GDANTIVCNS
62
KDGGAWGTEQ
72
REAVFPFQPG
82
SVAEVITFDQ
93
ANLTVKLPDG
103

YEFKFPNRLN
113
LEAINYMAAD
123
GDFKIKVAFD
134
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CME or .CME2 or .CME3 or :3CME;style chemicals stick;color identity;select .A:11 or .A:14 or .A:15 or .A:17 or .A:18 or .A:19 or .A:20 or .A:21 or .A:86 or .A:87 or .A:89 or .A:90 or .A:97 or .A:98 or .A:99 or .A:100 or .A:101 or .A:102 or .A:128 or .A:129 or .A:131 or .A:132 or .A:133 or .A:134; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU11
3.362
GLY14
3.971
GLU15
1.329
LEU17
1.330
ARG18
2.468
VAL19
2.609
ARG20
2.064
GLY21
4.290
GLU86
2.414
VAL87
1.331
ILE89
1.331
THR90
2.852
Residue
Distance (Å)
THR97
3.676
VAL98
2.781
LYS99
1.842
LEU100
3.179
PRO101
2.465
ASP102
4.724
ILE128
2.811
LYS129
1.329
VAL131
1.332
ALA132
3.058
PHE133
2.814
ASP134
1.821
References  Top
REF 1 Taloside inhibitors of galectin-1 and galectin-3. Chem Biol Drug Des. 2012 Mar;79(3):339-46.
REF 2 Galectin-1 in Complex with Ligand AN020
REF 3 Galectin-1 in Complex with Ligand NB169
REF 4 Galectin-1 in Complex with Ligand AN027
REF 5 Aromatic heterocycle galectin-1 interactions for selective single-digit nM affinity ligands
REF 6 Galectin-1 in Complex with Ligand JB60
REF 7 Galectin-1 in complex with 4-Amino-6-chloro-1,3-benzenedisulfonamide
REF 8 Structural insights into the redesign of a sucrose phosphorylase by induced loop repositioning

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