Structure of PDB 2c3q Chain D

Receptor sequence
>2c3qD (length=239) Species: 9606 (Homo sapiens) [Search protein sequence]
GLELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPL
KKVPALKDGDFTLTESVAILLYLTRKYKVPDYWYPQDLQARARVDEYLAW
QHTTLRRSCLRALWHKVMFPVFLGEPVSPQTLAATLAELDVTLQLLEDKF
LQNKAFLTGPHISLADLVAITELMHPVGAGCQVFEGRPKLATWRQRVEAA
VGEDLFQEAHEVILKAKDFPPADPTIKQKLMPRVLAMIR
3D structure
PDB2c3q Structural Basis of the Suppressed Catalytic Activity of Wild-Type Human Glutathione Transferase T1-1 Compared to its W234R Mutant.
ChainD
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S11
Catalytic site (residue number reindexed from 1) S10
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 GTX D S11 L35 H40 K53 V54 E66 S67 R234 M238 S10 L34 H39 K52 V53 E65 S66 R233 M237
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0004602 glutathione peroxidase activity
GO:0005515 protein binding
GO:0016740 transferase activity
Biological Process
GO:0006749 glutathione metabolic process
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome

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Cellular Component
External links
PDB RCSB:2c3q, PDBe:2c3q, PDBj:2c3q
PDBsum2c3q
PubMed16298388
UniProtP30711|GSTT1_HUMAN Glutathione S-transferase theta-1 (Gene Name=GSTT1)

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