Structure of PDB 3ik7 Chain A

Receptor sequence
>3ik7A (length=221) Species: 9606 (Homo sapiens) [Search protein sequence]
AARPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYKLQDGNHLL
FQQVPMVEIDGMKLVQTRSILHYIADKHNLFGKNLKERTLIDMYVEGTLD
LLELLIMHPFLKPDDQQKEVVNMAQKAIIRYFPVFEKILRGHGQSFLVGN
QLSLADVILLQTILALEEKIPNILSAFPFLQEYTVKLSNIPTIKRFLEPG
SKKKPPPDEIYVRTVYNIFRP
3D structure
PDB3ik7 Substrate specificity combined with stereopromiscuity in glutathione transferase A4-4-dependent metabolism of 4-hydroxynonenal.
ChainA
Resolution1.97 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y9 R15 R20
Catalytic site (residue number reindexed from 1) Y8 R14 R19
Enzyme Commision number 2.5.1.18: glutathione transferase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 BOB A Y9 R15 Q54 V55 Q67 T68 F111 Y212 F220 Y8 R14 Q53 V54 Q66 T67 F110 Y211 F219
BS02 BOB A D101 R131 D100 R130
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0005515 protein binding
GO:0016740 transferase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006749 glutathione metabolic process
GO:0006805 xenobiotic metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3ik7, PDBe:3ik7, PDBj:3ik7
PDBsum3ik7
PubMed20085333
UniProtO15217|GSTA4_HUMAN Glutathione S-transferase A4 (Gene Name=GSTA4)

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