Structure of PDB 2f3m Chain A Binding Site BS01

Receptor Information
>2f3m Chain A (length=218) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MPMILGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEK
FKLGLDFPNLPYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDIL
ENQTMDNHMQLGMICYNPEFEKLKPKYLEELPEKLKLYSEFLGKRPWFAG
NKITFVDFLVYDVLDLHRIFEPKCLDAFPNLKDFISRFEGLEKISAYMKS
SRFLPRPVFSKMAVWGNK
Ligand information
Ligand IDGTD
InChIInChI=1S/C16H20N6O12S/c17-8(16(27)28)1-2-12(23)19-9(15(26)18-5-13(24)25)6-35-14-10(21(31)32)3-7(20(29)30)4-11(14)22(33)34/h3-4,7-9,14H,1-2,5-6,17H2,(H,18,26)(H,19,23)(H,24,25)(H,27,28)/t7-,8-,9-,14+/m0/s1
InChIKeyVQUXYLXGOSJDJJ-OSGJSWLFSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=[N+]([O-])C1=CC([N+]([O-])=O)C=C([N+]([O-])=O)C1SCC(C(=O)NCC(=O)O)NC(=O)CCC(C(=O)O)N
CACTVS 3.341N[C@@H](CCC(=O)N[C@@H](CS[C@@H]1C(=C[C@@H](C=C1[N+]([O-])=O)[N+]([O-])=O)[N+]([O-])=O)C(=O)NCC(O)=O)C(O)=O
OpenEye OEToolkits 1.5.0C1=C(C(C(=CC1[N+](=O)[O-])[N+](=O)[O-])SCC(C(=O)NCC(=O)O)NC(=O)CCC(C(=O)O)N)[N+](=O)[O-]
CACTVS 3.341N[CH](CCC(=O)N[CH](CS[CH]1C(=C[CH](C=C1[N+]([O-])=O)[N+]([O-])=O)[N+]([O-])=O)C(=O)NCC(O)=O)C(O)=O
OpenEye OEToolkits 1.5.0C1=C(C(C(=CC1[N+](=O)[O-])[N+](=O)[O-])SC[C@@H](C(=O)NCC(=O)O)NC(=O)CC[C@@H](C(=O)O)N)[N+](=O)[O-]
FormulaC16 H20 N6 O12 S
Name1-(S-GLUTATHIONYL)-2,4,6-TRINITROCYCLOHEXA-2,5-DIENE;
(S)-2-AMINO-5-((R)-1-(CARBOXYMETHYLAMINO)-1-OXO-3-(2,4,6-TRINITROCYCLOHEXA-2,5-DIENYLTHIO)PROPAN-2-YLAMINO)-5-OXOPENTANOIC ACID
ChEMBL
DrugBank
ZINC
PDB chain2f3m Chain A Residue 1218 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2f3m Transition state model and mechanism of nucleophilic aromatic substitution reactions catalyzed by human glutathione S-transferase M1a-1a.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		W45 K49 N58 L59 Q71 S72 Y115
Binding residue
(residue number reindexed from 1)		W46 K50 N59 L60 Q72 S73 Y116
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) Y6 L12
Catalytic site (residue number reindexed from 1) Y7 L13
Enzyme Commision number 2.5.1.18: glutathione transferase.
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016740 transferase activity
GO:0019899 enzyme binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0043295 glutathione binding
Biological Process
GO:0006629 lipid metabolic process
GO:0006693 prostaglandin metabolic process
GO:0006749 glutathione metabolic process
GO:0018916 nitrobenzene metabolic process
GO:0042178 xenobiotic catabolic process
GO:0051122 hepoxilin biosynthetic process
GO:0070458 cellular detoxification of nitrogen compound
GO:1901687 glutathione derivative biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0045171 intercellular bridge

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2f3m, PDBe:2f3m, PDBj:2f3m
PDBsum2f3m
PubMed16548513
UniProtP09488|GSTM1_HUMAN Glutathione S-transferase Mu 1 (Gene Name=GSTM1)

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