Binding Site Information of Target

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Target 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
Drug Binding Sites of Target  Top
Ligand Name: Cysteine Sulfenic Acid Ligand Info
Structure Description X-RAY CRYSTAL STRUCTURE OF C2S HUMAN GALECTIN-1 COMPLEXED WITH GALACTOSE PDB:1W6M
Method X-ray diffraction Resolution 2.30 Å Mutation Yes [1]
PDB Sequence
ASGLVASNLN
1010
LKPGELRVRG
1021
EVAPDAKSFV
1031
LNLGKDSNNL
1041
CLHFNPRFNA
1051

HGDANTIVCN
1061
SKDDGAWGTE
1071
QREAVFPFQP
1081
GSVAEVCITF
1091
DQANLTVKLP
1101

DGYEFKFPNR
1111
LNLEAINYMA
1121
ADGDFKIKCV
1131
AFD
Residue
Distance (Å)
LEU1011
4.429
GLY1014
3.960
GLU1015
1.329
LEU1017
1.327
ARG1018
3.945
CYS1088
3.756
Residue
Distance (Å)
ILE1089
3.521
THR1090
3.628
ALA1132
3.833
PHE1133
3.709
ASP1134
3.174
Ligand Name: S,S-(2-Hydroxyethyl)Thiocysteine Ligand Info
Structure Description Galectin-1 in Complex with Ligand JB60 PDB:5MWX
Method X-ray diffraction Resolution 1.29 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
3.140
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
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Methyl 2-O-Acetyl-3-O-(4-Methylbenzoyl)-Beta-D-Talopyranoside Ligand Info
Structure Description Crystal structure of human galectin-1 in complex with methyl 2-O-acetyl-3-O-toluoyl-beta-D-talopyranoside PDB:3T2T
Method X-ray diffraction Resolution 1.90 Å Mutation No [3]
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
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .MQT or .MQT2 or .MQT3 or :3MQT;style chemicals stick;color identity;select .A:29 or .A:31 or .A:44 or .A:46 or .A:48 or .A:52 or .A:59 or .A:61 or .A:68 or .A:71 or .A:123 or .A:124; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER29
4.351
VAL31
3.607
HIS44
2.627
ASN46
3.678
ARG48
3.482
HIS52
3.205
Residue
Distance (Å)
VAL59
4.225
ASN61
2.822
TRP68
3.874
GLU71
2.691
ASP123
3.192
GLY124
3.951
Ligand Name: Prop-2-En-1-Yl 2-(Acetylamino)-4-O-(3-O-{[1-(5-Amino-1h-1,2,4-Triazol-3-Yl)-1h-1,2,3-Triazol-4-Yl]methyl}-Beta-D-Galactopyranosyl)-2-Deoxy-Beta-D-Glucopyranoside Ligand Info
Structure Description Galectin-1 in Complex with Ligand AN020 PDB:4Q2F
Method X-ray diffraction Resolution 1.40 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 .2XW or .2XW2 or .2XW3 or :32XW;style chemicals stick;color identity;select .A:29 or .A:30 or .A:31 or .A:44 or .A:46 or .A:48 or .A:52 or .A:54 or .A:59 or .A:61 or .A:68 or .A:69 or .A:71 or .A:73 or .A:123 or .A:124 or .A:125; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER29
2.418
PHE30
2.661
VAL31
2.769
HIS44
1.389
ASN46
3.027
ARG48
2.138
HIS52
2.510
ASP54
4.057
VAL59
2.832
Residue
Distance (Å)
ASN61
1.684
TRP68
2.695
GLY69
4.756
GLU71
1.758
ARG73
2.154
ASP123
2.895
GLY124
1.869
ASP125
3.302
Ligand Name: Propyl 2-(Acetylamino)-4-O-{3-O-[(1-Benzyl-1h-1,2,3-Triazol-4-Yl)methyl]-Beta-D-Galactopyranosyl}-2-Deoxy-Beta-D-Glucopyranoside Ligand Info
Structure Description Galectin-1 in Complex with Ligand NB169 PDB:4Q1P
Method X-ray diffraction Resolution 1.46 Å Mutation No [5]
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 .2XT or .2XT2 or .2XT3 or :32XT;style chemicals stick;color identity;select .A:29 or .A:30 or .A:31 or .A:33 or .A:44 or .A:46 or .A:48 or .A:52 or .A:54 or .A:59 or .A:60 or .A:61 or .A:68 or .A:71 or .A:73 or .A:123 or .A:124 or .A:125; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER29
3.339
PHE30
4.567
VAL31
2.914
ASN33
4.238
HIS44
1.988
ASN46
3.219
ARG48
2.003
HIS52
3.043
ASP54
4.751
Residue
Distance (Å)
VAL59
3.815
CYS60
4.974
ASN61
2.144
TRP68
3.146
GLU71
2.706
ARG73
2.917
ASP123
3.668
GLY124
3.003
ASP125
4.553
Ligand Name: Propyl 2-(Acetylamino)-2-Deoxy-4-O-[3-O-({1-[2-(3-Hydroxyphenyl)-2-Oxoethyl]-1h-1,2,3-Triazol-4-Yl}methyl)-Beta-D-Galactopyranosyl]-Beta-D-Glucopyranoside Ligand Info
Structure Description Galectin-1 in Complex with Ligand AN027 PDB:4Q1R
Method X-ray diffraction Resolution 1.47 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 .2XU or .2XU2 or .2XU3 or :32XU;style chemicals stick;color identity;select .A:28 or .A:29 or .A:30 or .A:31 or .A:33 or .A:44 or .A:46 or .A:48 or .A:52 or .A:54 or .A:59 or .A:60 or .A:61 or .A:68 or .A:71 or .A:73 or .A:123 or .A:124 or .A:125; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS28
3.845
SER29
2.912
PHE30
4.349
VAL31
2.844
ASN33
4.179
HIS44
1.994
ASN46
3.272
ARG48
1.915
HIS52
3.202
ASP54
4.613
Residue
Distance (Å)
VAL59
3.834
CYS60
4.932
ASN61
2.032
TRP68
3.137
GLU71
2.776
ARG73
2.828
ASP123
3.158
GLY124
2.725
ASP125
3.102
Ligand Name: 3-Deoxy-3-[4-(Thiophen-3-Yl)-1h-1,2,3-Triazol-1-Yl]-Beta-D-Galactopyranosyl 3-Deoxy-1-Thio-3-[4-(Thiophen-3-Yl)-1h-1,2,3-Triazol-1-Yl]-Beta-D-Galactopyranoside Ligand Info
Structure Description Crystal Structure of Human Galectin-1 in Complex With Thienyl-1,2, 3-triazolyl Thiodigalactoside Inhibitor PDB:6F83
Method X-ray diffraction Resolution 2.20 Å Mutation No [7]
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 .5KT or .5KT2 or .5KT3 or :35KT;style chemicals stick;color identity;select .A:29 or .A:30 or .A:31 or .A:44 or .A:46 or .A:48 or .A:52 or .A:53 or .A:54 or .A:59 or .A:61 or .A:68 or .A:71 or .A:73 or .A:123 or .A:124; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER29
3.428
PHE30
4.609
VAL31
3.258
HIS44
2.639
ASN46
3.295
ARG48
3.001
HIS52
3.426
GLY53
4.214
Residue
Distance (Å)
ASP54
4.125
VAL59
4.703
ASN61
3.039
TRP68
3.837
GLU71
2.600
ARG73
3.304
ASP123
3.636
GLY124
3.488
Ligand Name: beta-D-galactose Ligand Info
Structure Description X-RAY CRYSTAL STRUCTURE OF C2S HUMAN GALECTIN-1 COMPLEXED WITH GALACTOSE PDB:1W6M
Method X-ray diffraction Resolution 2.30 Å Mutation Yes [1]
PDB Sequence
> Chain A
ASGLVASNLN
1010
LKPGELRVRG
1021
EVAPDAKSFV
1031
LNLGKDSNNL
1041
CLHFNPRFNA
1051

HGDANTIVCN
1061
SKDDGAWGTE
1071
QREAVFPFQP
1081
GSVAEVCITF
1091
DQANLTVKLP
1101

DGYEFKFPNR
1111
LNLEAINYMA
1121
ADGDFKIKCV
1131
AFD
> Chain B
ASGLVASNLN
2010
LKPGECLRVR
2020
GEVAPDAKSF
2030
VLNLGKDSNN
2040
LCLHFNPRFN
2050

AHGDANTIVC
2060
NSKDDGAWGT
2070
EQREAVFPFQ
2080
PGSVAEVCIT
2090
FDQANLTVKL
2100

PDGYEFKFPN
2110
RLNLEAINYM
2120
AADGDFKIKC
2130
VAFD
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GAL or .GAL2 or .GAL3 or :3GAL;style chemicals stick;color identity;select .A:1044 or .A:1046 or .A:1048 or .A:1052 or .A:1061 or .A:1068 or .A:1071 or .B:2044 or .B:2046 or .B:2048 or .B:2052 or .B:2059 or .B:2061 or .B:2068 or .B:2069 or .B:2071; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
HIS1044[A]
2.689
ASN1046[A]
3.396
ARG1048[A]
2.998
HIS1052[A]
3.050
ASN1061[A]
2.882
TRP1068[A]
3.946
GLU1071[A]
2.795
HIS2044[B]
3.378
Residue
Distance (Å)
ASN2046[B]
4.990
ARG2048[B]
3.097
HIS2052[B]
4.244
VAL2059[B]
4.976
ASN2061[B]
2.657
TRP2068[B]
3.685
GLY2069[B]
4.942
GLU2071[B]
2.603
Ligand Name: N-[(2R,3R,4R,5S,6R)-5-[(2S,3R,4S,5S,6R)-4-[[1-[[3-(3-aminoprop-1-ynyl)phenyl]methyl]triazol-4-yl]methoxy]-3,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-4-hydroxy-6-(hydroxymethyl)-2-propoxyoxan-3-yl]acetamide Ligand Info
Structure Description Galectin-1 in Complex with Ligand JB60 PDB:5MWX
Method X-ray diffraction Resolution 1.29 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
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .WYD or .WYD2 or .WYD3 or :3WYD;style chemicals stick;color identity;select .A:28 or .A:29 or .A:30 or .A:31 or .A:33 or .A:44 or .A:46 or .A:48 or .A:52 or .A:54 or .A:59 or .A:60 or .A:61 or .A:68 or .A:71 or .A:73 or .A:123 or .A:124 or .A:125; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS28
4.774
SER29
3.074
PHE30
4.923
VAL31
3.108
ASN33
3.963
HIS44
1.867
ASN46
3.242
ARG48
2.155
HIS52
3.022
ASP54
4.915
Residue
Distance (Å)
VAL59
3.794
CYS60
4.953
ASN61
2.033
TRP68
3.270
GLU71
2.693
ARG73
2.813
ASP123
3.659
GLY124
2.543
ASP125
2.899
Ligand Name: 3-Deoxy-3-[4-(3-Fluorophenyl)-1h-1,2,3-Triazol-1-Yl]-Beta-D-Galactopyranosyl 3-Deoxy-3-[4-(3-Fluorophenyl)-1h-1,2,3-Triazol-1-Yl]-1-Thio-Beta-D-Galactopyranoside Ligand Info
Structure Description Complex of human Galectin-1 and TD-139 PDB:4Y24
Method X-ray diffraction Resolution 2.32 Å Mutation No [8]
PDB Sequence
CGLVASNLNL
11
KPGECLRVRG
21
EVAPDAKSFV
31
LNLGKDSNNL
41
CLHFNPRFNA
51

HGDANTIVCN
61
SKDGGAWGTE
71
QREAVFPFQP
81
GSVAEVCITF
91
DQANLTVKLP
101

DGYEFKFPNR
111
LNLEAINYMA
121
ADGDFKIKCV
131
AFD
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .TD2 or .TD22 or .TD23 or :3TD2;style chemicals stick;color identity;select .A:29 or .A:30 or .A:31 or .A:44 or .A:46 or .A:48 or .A:52 or .A:53 or .A:54 or .A:59 or .A:61 or .A:68 or .A:71 or .A:73 or .A:123 or .A:124; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER29
3.202
PHE30
3.628
VAL31
3.324
HIS44
2.675
ASN46
3.728
ARG48
3.044
HIS52
3.778
GLY53
4.499
Residue
Distance (Å)
ASP54
2.957
VAL59
4.122
ASN61
2.969
TRP68
3.698
GLU71
2.368
ARG73
3.169
ASP123
3.913
GLY124
3.601
Ligand Name: ~{N}-[(2~{R},3~{R},4~{R},5~{S},6~{R})-5-[(2~{S},3~{R},4~{S},5~{S},6~{R})-4-[[1-[[3-[(~{Z})-3-[bis(azanyl)methylideneamino]prop-1-enyl]phenyl]methyl]-1,2,3-triazol-4-yl]methoxy]-6-(hydroxymethyl)-3,5-bis(oxidanyl)oxan-2-yl]oxy-6-(hydroxymethyl)-4-oxidanyl-2-prop-2-enoxy-oxan-3-yl]ethanamide Ligand Info
Structure Description Galectin-1 in Complex with Ligand JB97 PDB:5MWT
Method X-ray diffraction Resolution 1.71 Å Mutation No [9]
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 .JB9 or .JB92 or .JB93 or :3JB9;style chemicals stick;color identity;select .A:29 or .A:30 or .A:31 or .A:33 or .A:44 or .A:46 or .A:48 or .A:52 or .A:54 or .A:59 or .A:61 or .A:68 or .A:71 or .A:73 or .A:123 or .A:124 or .A:125 or .A:126; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER29
3.398
PHE30
4.604
VAL31
2.851
ASN33
4.071
HIS44
1.996
ASN46
3.336
ARG48
2.033
HIS52
2.764
ASP54
4.688
Residue
Distance (Å)
VAL59
3.790
ASN61
2.159
TRP68
3.309
GLU71
2.647
ARG73
2.820
ASP123
3.372
GLY124
2.651
ASP125
2.778
PHE126
4.559
References  Top
REF 1 Growth-regulatory human galectin-1: crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding. J Mol Biol. 2004 Oct 29;343(4):957-70.
REF 2 Galectin-1 in Complex with Ligand JB60
REF 3 Taloside inhibitors of galectin-1 and galectin-3. Chem Biol Drug Des. 2012 Mar;79(3):339-46.
REF 4 Galectin-1 in Complex with Ligand AN020
REF 5 Galectin-1 in Complex with Ligand NB169
REF 6 Galectin-1 in Complex with Ligand AN027
REF 7 Aromatic heterocycle galectin-1 interactions for selective single-digit nM affinity ligands
REF 8 Dual thio-digalactoside-binding modes of human galectins as the structural basis for the design of potent and selective inhibitors. Sci Rep. 2016 Jul 15;6:29457.
REF 9 Structural insights into the redesign of a sucrose phosphorylase by induced loop repositioning

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