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Receptor Information

>3ik9 Chain F (length=216) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

KPKLHYFNGRGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQ
QVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYIEGIADLG
EMIIMLPFCPPEEKDAKLALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKL
SRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSP
RKPPPDEIYVRTVYNI

Ligand ID

BOB

InChI

InChI=1S/C19H35N3O8S/c1-2-3-4-5-14(24)15(8-9-23)31-11-13(18(28)21-10-17(26)27)22-16(25)7-6-12(20)19(29)30/h12-15,23-24H,2-11,20H2,1H3,(H,21,28)(H,22,25)(H,26,27)(H,29,30)/t12-,13-,14+,15-/m0/s1

InChIKey

CLEVVMDJDMEQKG-XQLPTFJDSA-N

SMILES

Software	SMILES
CACTVS 3.352	CCCCC[CH](O)[CH](CCO)SC[CH](NC(=O)CC[CH](N)C(O)=O)C(=O)NCC(O)=O
CACTVS 3.352	CCCCC[C@@H](O)[C@H](CCO)SC[C@H](NC(=O)CC[C@H](N)C(O)=O)C(=O)NCC(O)=O
OpenEye OEToolkits 1.7.0	CCCCCC(C(CCO)SCC(C(=O)NCC(=O)O)NC(=O)CCC(C(=O)O)N)O
OpenEye OEToolkits 1.7.0	CCCCC[C@H]([C@H](CCO)SC[C@@H](C(=O)NCC(=O)O)NC(=O)CC[C@@H](C(=O)O)N)O
ACDLabs 11.02	O=C(NC(C(=O)NCC(=O)O)CSC(C(O)CCCCC)CCO)CCC(C(=O)O)N

Formula

C19 H35 N3 O8 S

Name

(S)-2-amino-5-((R)-1-(carboxymethylamino)-3-((3S,4R)-1,4-dihydroxynonan-3-ylthio)-1-oxopropan-2-ylamino)-5-oxopentanoic acid;
L-gamma-glutamyl-S-[(1S,2R)-2-hydroxy-1-(2-hydroxyethyl)heptyl]-L-cysteinylglycine

PDB chain

3ik9 Chain F Residue 506 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	3ik9 Substrate specificity combined with stereopromiscuity in glutathione transferase A4-4-dependent metabolism of 4-hydroxynonenal.
Resolution	2.2 Å
Binding residue (original residue number in PDB)	Y9 R15 Q54 V55 Q67 T68 F111 Y212
Binding residue (residue number reindexed from 1)	Y6 R12 Q51 V52 Q64 T65 F108 Y209
Annotation score	2

Catalytic site (original residue number in PDB)	Y9 R15 R20
Catalytic site (residue number reindexed from 1)	Y6 R12 R17
Enzyme Commision number	1.11.1.- 2.5.1.18: glutathione transferase. 5.3.3.-

	Molecular Function
GO:0004364	glutathione transferase activity
GO:0004601	peroxidase activity
GO:0004602	glutathione peroxidase activity
GO:0004769	steroid delta-isomerase activity
GO:0005504	fatty acid binding
GO:0005515	protein binding
GO:0016740	transferase activity
GO:0016853	isomerase activity

	Biological Process
GO:0006629	lipid metabolic process
GO:0006693	prostaglandin metabolic process
GO:0006749	glutathione metabolic process
GO:0006805	xenobiotic metabolic process
GO:0030855	epithelial cell differentiation
GO:0043651	linoleic acid metabolic process
GO:0098869	cellular oxidant detoxification
GO:1901687	glutathione derivative biosynthetic process

	Cellular Component
GO:0005737	cytoplasm
GO:0005829	cytosol
GO:0070062	extracellular exosome

PDB	RCSB:3ik9, PDBe:3ik9, PDBj:3ik9
PDBsum	3ik9
PubMed	20085333
UniProt	P08263\|GSTA1_HUMAN Glutathione S-transferase A1 (Gene Name=GSTA1)

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Structure of PDB 3ik9 Chain F Binding Site BS02