Structure of PDB 3cru Chain A

Receptor sequence
>3cruA (length=214) Species: 6182 (Schistosoma japonicum) [Search protein sequence]
MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGC
EFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVL
DIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTH
PDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIA
WPLQGWQATFGGGD
3D structure
PDB3cru Using affinity chromatography to engineer and characterize pH-dependent protein switches.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Y7 L13
Catalytic site (residue number reindexed from 1) Y7 L13
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 Y7 W8 L13 N54 L55 Q67 S68 Y7 W8 L13 N54 L55 Q67 S68
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016740 transferase activity
Biological Process
GO:0006749 glutathione metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3cru, PDBe:3cru, PDBj:3cru
PDBsum3cru
PubMed19177365
UniProtP08515|GST26_SCHJA Glutathione S-transferase class-mu 26 kDa isozyme

[Back to BioLiP]