Structure of PDB 4ri7 Chain B

Receptor sequence
>4ri7B (length=214) Species: 47664 (Populus tremula x Populus tremuloides) [Search protein sequence]
ATPVTIYGPPLCTAVSRVLATLIEKDVPFHLIPIDLSKGEQKKPEYLKIQ
PFGQVPAFKDESITLFESRAICRYICDKYADKGNKSLYGTDILSKANIDQ
WVETDGQTFGPPSGDLVHDLLFSSVPVDEALIKKNVDKLAKVLDIYEQKL
GQTRFLAGDEFSFADLSHLPNGDYLVNSTDKGYLFTSRKNVNRWWTEISN
RESWKKVLEMRKNA
3D structure
PDB4ri7 The poplar Phi class glutathione transferase: expression, activity and structure of GSTF1.
ChainB
Resolution1.798 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) C13
Catalytic site (residue number reindexed from 1) C12
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 B C13 A15 Q42 K43 Q55 V56 E68 S69 C12 A14 Q41 K42 Q54 V55 E67 S68
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016740 transferase activity
GO:0043295 glutathione binding
Biological Process
GO:0006749 glutathione metabolic process
GO:0009407 toxin catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4ri7, PDBe:4ri7, PDBj:4ri7
PDBsum4ri7
PubMed25566286
UniProtA9PHH6

[Back to BioLiP]