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 T21669 Target Info
Target Name Glutathione S-transferase P (GSTP1)
Synonyms GSTP11; GSTP1-1; GST3; GST classpi; GST class-pi; FAEES3
Target Type Clinical trial Target
Gene Name GSTP1
Biochemical Class Alkyl aryl transferase
UniProt ID
GSTP1_HUMAN
Ligand General Information  Top
Ligand Name 2-Amino-4-[1-(carboxymethyl-carbamoyl)-2-(9-hydroxy-7,8-dioxo-7,8,9,10-tetrahydro-benzo[def]chrysen-10-ylsulfanyl)-ethylcarbamoyl]-butyric acid Ligand Info
Canonical SMILES C1=CC2=C3C(=C1)C=CC4=C3C(=CC5=C4C(C(C(=O)C5=O)O)SCC(C(=O)NCC(=O)O)NC(=O)CCC(C(=O)O)N)C=C2
InChI 1S/C30H27N3O9S/c31-18(30(41)42)8-9-20(34)33-19(29(40)32-11-21(35)36)12-43-28-24-16-7-6-14-3-1-2-13-4-5-15(23(16)22(13)14)10-17(24)25(37)26(38)27(28)39/h1-7,10,18-19,27-28,39H,8-9,11-12,31H2,(H,32,40)(H,33,34)(H,35,36)(H,41,42)/t18-,19-,27-,28-/m0/s1
InChIKey DUWOHLGCRJLRRU-HVYZTVOGSA-N
PubChem Compound ID 5288368
Drug Binding Sites of Target  Top
PDB ID: 4PGT      CRYSTAL STRUCTURE OF HGSTP1-1[V104] COMPLEXED WITH THE GSH CONJUGATE OF (+)-ANTI-BPDE
Method X-ray diffraction Resolution 2.10 Å Mutation Yes [1]
PDB Sequence
MPPYTVVYFP
9
VRGRCAALRM
19
LLADQGQSWK
29
EEVVTVETWQ
39
EGSLKASCLY
49

GQLPKFQDGD
59
LTLYQSNTIL
69
RHLGRTLGLY
79
GKDQQEAALV
89
DMVNDGVEDL
99

RKYVSLIYTN
110
YEAGKDDYVK
120
ALPGQLKPFE
130
TLLSQNQGGK
140
TFIVGDQISF
150

ADYNLLDLLL
160
IHEVLAPGCL
170
DAFPLLSAYV
180
GRLSARPKLK
190
AFLASPEYVN
200

LPINGNGKQ
Residue
Distance (Å)
TYR7
3.248
PHE8
3.439
VAL10
3.749
GLY12
4.533
ARG13
3.342
VAL35
4.398
TRP38
3.050
LYS44
2.695
GLY50
3.922
GLN51
2.853
Residue
Distance (Å)
LEU52
2.700
PRO53
3.554
GLN64
2.757
SER65
2.748
ASN66
4.551
VAL104
3.808
TYR108
3.299
ASN204
4.928
GLY205
3.594
ASN206
4.866
PDB ID: 3PGT      CRYSTAL STRUCTURE OF HGSTP1-1[I104] COMPLEXED WITH THE GSH CONJUGATE OF (+)-ANTI-BPDE
Method X-ray diffraction Resolution 2.14 Å Mutation No [1]
PDB Sequence
MPPYTVVYFP
9
VRGRCAALRM
19
LLADQGQSWK
29
EEVVTVETWQ
39
EGSLKASCLY
49

GQLPKFQDGD
59
LTLYQSNTIL
69
RHLGRTLGLY
79
GKDQQEAALV
89
DMVNDGVEDL
99

RCKYISLIYT
109
NYEAGKDDYV
119
KALPGQLKPF
129
ETLLSQNQGG
139
KTFIVGDQIS
149

FADYNLLDLL
159
LIHEVLAPGC
169
LDAFPLLSAY
179
VGRLSARPKL
189
KAFLASPEYV
199

NLPINGNGKQ
209
Residue
Distance (Å)
PHE8
3.375
PRO9
4.610
VAL10
3.649
ARG13
3.331
TRP38
2.910
LYS44
2.835
GLY50
3.999
GLN51
3.112
LEU52
2.756
Residue
Distance (Å)
PRO53
3.659
GLN64
2.621
SER65
2.830
ASN66
4.681
ILE104
3.948
TYR108
3.281
GLY205
2.799
ASN206
4.059
References  Top
REF 1 Structure and function of residue 104 and water molecules in the xenobiotic substrate-binding site in human glutathione S-transferase P1-1. Biochemistry. 1999 Aug 10;38(32):10231-8.

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