Structure of PDB 1u87 Chain A

Receptor sequence
>1u87A (length=209) Species: 6182 (Schistosoma japonicum) [Search protein sequence]
MSPILGFWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGL
EFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVL
DIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTH
PDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIA
WPLQGWQAT
3D structure
PDB1u87 Crystallographic and Thermodynamic Analysis of the Binding of S-Octylglutathione to the Tyr 7 to Phe Mutant of Glutathione S-Transferase from Schistosoma japonicum(,)
ChainA
Resolution3.5 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) F7 L13
Catalytic site (residue number reindexed from 1) F7 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 N54 L55 Q67 S68 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:1u87, PDBe:1u87, PDBj:1u87
PDBsum1u87
PubMed15667211
UniProtP08515|GST26_SCHJA Glutathione S-transferase class-mu 26 kDa isozyme

[Back to BioLiP]