Structure of PDB 1gul Chain E

Receptor sequence
>1gulE (length=217) Species: 9606 (Homo sapiens) [Search protein sequence]
RPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYKLQDGNHLLFQ
QVPMVEIDGMKLVQTRSILHYIADKHNLFGKNLKERTLIDMYVEGTLDLL
ELLIMHPFLKPDDQQKEVVNMAQKAIIRYFPVFEKILRGHGQSFLVGNQL
SLADVILLQTILALEEKIPNILSAFPFLQEYTVKLSNIPTIKRFLEPGSK
KKPPPDEIYVRTVYNIF
3D structure
PDB1gul Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products
ChainE
Resolution2.7 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) Y6 R12 R17
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 IBG E Q54 V55 Q67 T68 F220 Q51 V52 Q64 T65 F217
BS02 IBG E D101 R131 D98 R128
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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Cellular Component
External links
PDB RCSB:1gul, PDBe:1gul, PDBj:1gul
PDBsum1gul
PubMed10329152
UniProtO15217|GSTA4_HUMAN Glutathione S-transferase A4 (Gene Name=GSTA4)

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