Structure of PDB 2caq Chain A

Receptor sequence
>2caqA (length=204) Species: 6185 (Schistosoma haematobium) [Search protein sequence]
DHIKVIYFNGRGRAESILMTLVAAGVNYEDERISFQDWPKIKPTIPGGRL
PAVKITDNHGHVKWMVESLAIARYMAKKHHMMGGTEEEYYNVEKLIGQAE
DLEHEYYKTLMKPEEEKQKIIKEILNGKVPVLLDIICESLKASTGKLAVG
DKVTLADLVLIAVIDHVTDLDKEFLTGKYPEIHKHRENLLASSPRLAKYL
SDRA
3D structure
PDB2caq Probing the Mechanism of Gsh Activation in Schistosoma Haematobium Glutathione-S-Transferase by Site-Directed Mutagenesis and X-Ray Crystallography.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y10 R16 L21
Catalytic site (residue number reindexed from 1) Y7 R13 L18
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 F11 R16 W41 K45 G51 R52 L53 E70 S71 F8 R13 W38 K42 G48 R49 L50 E67 S68 MOAD: Kd=285uM
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016740 transferase activity
Biological Process
GO:0006749 glutathione metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2caq, PDBe:2caq, PDBj:2caq
PDBsum2caq
PubMed16777141
UniProtP30113|GST28_SCHHA Glutathione S-transferase class-mu 28 kDa isozyme

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