Structure of PDB 3gur Chain A Binding Site BS01

Receptor Information
>3gur Chain A (length=217) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PMTLGYWNIRGLAHSIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKF
KLGLDFPNLPYLIDGTHKITQSNAILRYIARKHNLCGESEKEQIREDILE
NQFMDSRMQLAKLCYDPDFEKLKPEYLQALPEMLKLYSQFLGKQPWFLGD
KITFVDFIAYDVLERNQVFEPSCLDAFPNLKDFISRFEGLEKISAYMKSS
RFLPRPVFTKMAVWGNK
Ligand information
Ligand IDBYG
InChIInChI=1S/C22H32N6O10S2/c23-13(21(34)35)5-6-16(30)25-14(20(33)24-11-17(31)32)12-40-22(39-10-4-2-1-3-9-29)8-7-15(28(36)37)18-19(22)27-38-26-18/h7,13-14,29H,1-6,8-12,23H2,(H,24,33)(H,25,30)(H,31,32)(H,34,35)/t13-,14-,22+/m0/s1
InChIKeyDZIARIAPFJPVSN-FBJOKTGGSA-N
SMILES
SoftwareSMILES
CACTVS 3.352N[CH](CCC(=O)N[CH](CS[C]1(CC=C(c2nonc12)[N+]([O-])=O)SCCCCCCO)C(=O)NCC(O)=O)C(O)=O
OpenEye OEToolkits 1.7.0C1C=C(c2c(non2)[C@]1(SCCCCCCO)SC[C@@H](C(=O)NCC(=O)O)NC(=O)CC[C@@H](C(=O)O)N)[N+](=O)[O-]
ACDLabs 11.02O=C(O)C(N)CCC(=O)NC(C(=O)NCC(=O)O)CSC1(SCCCCCCO)c2nonc2C(=CC1)[N+]([O-])=O
CACTVS 3.352N[C@@H](CCC(=O)N[C@@H](CS[C@@]1(CC=C(c2nonc12)[N+]([O-])=O)SCCCCCCO)C(=O)NCC(O)=O)C(O)=O
OpenEye OEToolkits 1.7.0C1C=C(c2c(non2)C1(SCCCCCCO)SCC(C(=O)NCC(=O)O)NC(=O)CCC(C(=O)O)N)[N+](=O)[O-]
FormulaC22 H32 N6 O10 S2
NameL-gamma-glutamyl-S-{(4R)-4-[(6-hydroxyhexyl)sulfanyl]-7-nitro-4,5-dihydro-2,1,3-benzoxadiazol-4-yl}-L-cysteinylglycine
ChEMBL
DrugBank
ZINCZINC000058632614
PDB chain3gur Chain A Residue 218 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3gur Structural basis for the binding of the anticancer compound 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-transferases
Resolution2.5 Å
Binding residue
(original residue number in PDB)		Y6 W7 G11 L12 W45 K49 N58 L59 Q71 S72 R107 A111 Y115 F208 T209
Binding residue
(residue number reindexed from 1)		Y6 W7 G11 L12 W45 K49 N58 L59 Q71 S72 R107 A111 Y115 F208 T209
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=8.00,IC50=0.01uM
Enzymatic activity
Catalytic site (original residue number in PDB) Y6 L12 R17
Catalytic site (residue number reindexed from 1) Y6 L12 R17
Enzyme Commision number 2.5.1.18: glutathione transferase.
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0004602 glutathione peroxidase activity
GO:0005102 signaling receptor binding
GO:0005504 fatty acid binding
GO:0005515 protein binding
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:0006749 glutathione metabolic process
GO:0010880 regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
GO:0010881 regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
GO:0014809 regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
GO:0018916 nitrobenzene metabolic process
GO:0042178 xenobiotic catabolic process
GO:0043651 linoleic acid metabolic process
GO:0051122 hepoxilin biosynthetic process
GO:0055119 relaxation of cardiac muscle
GO:0060315 negative regulation of ryanodine-sensitive calcium-release channel activity
GO:0060316 positive regulation of ryanodine-sensitive calcium-release channel activity
GO:0070458 cellular detoxification of nitrogen compound
GO:0071313 cellular response to caffeine
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016529 sarcoplasmic reticulum
GO:0045171 intercellular bridge
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3gur, PDBe:3gur, PDBj:3gur
PDBsum3gur
PubMed19808963
UniProtP28161|GSTM2_HUMAN Glutathione S-transferase Mu 2 (Gene Name=GSTM2)

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