Structure of PDB 1tdi Chain A

Receptor sequence
>1tdiA (length=218) Species: 9606 (Homo sapiens) [Search protein sequence]
KPKLHYFNGRGRMEPIRWLLAAAGVEFEEKFIGSAEDLGKLRNDGSLMFQ
QVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYTEGMADLN
EMILLLPLCRPEEKDAKIALIKEKTKSRYFPAFEKVLQSHGQDYLVGNKL
SRADISLVELLYYVEELDSSLISNFPLLKALKTRISNLPTVKKFLQPGSP
RKPPADAKALEEARKIFR
3D structure
PDB1tdi Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid isomerase activity.
ChainA
Resolution2.4 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 GSH A R45 Q54 V55 Q67 T68 R42 Q51 V52 Q64 T65
BS02 GSH A D101 R131 D98 R128
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016740 transferase activity
Biological Process
GO:0006629 lipid metabolic process
GO:0006749 glutathione metabolic process
GO:0006805 xenobiotic metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome

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Cellular Component
External links
PDB RCSB:1tdi, PDBe:1tdi, PDBj:1tdi
PDBsum1tdi
PubMed15595823
UniProtQ16772|GSTA3_HUMAN Glutathione S-transferase A3 (Gene Name=GSTA3)

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