Structure of PDB 2vo4 Chain B

Receptor sequence
>2vo4B (length=219) Species: 3847 (Glycine max) [Search protein sequence]
MQDEVVLLDFWPSPFGMRVRIALAEKGIKYEYKEEDLRNKSPLLLQMNPV
HKKIPVLIHNGKPICESLIAVQYIEEVWNDRNPLLPSDPYQRAQTRFWAD
YVDKKIYDLGRKIWTSKGEEKEAAKKEFIEALKLLEEQLGDKTYFGGDNL
GFVDIALVPFYTWFKAYETFGTLNIESECPKFIAWAKRCLQKESVAKSLP
DQQKVYEFIMDLRKKLGIE
3D structure
PDB2vo4 Crystallographic and Functional Characterization of the Fluorodifen-Inducible Glutathione Transferase from Glycine Max Reveals an Active Site Topography Suited for Diphenylether Herbicides and a Novel L-Site.
ChainB
Resolution1.75 Å
3D
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
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 GTB B S13 F15 L37 K40 K53 I54 E66 S67 Y107 L212 L216 S13 F15 L37 K40 K53 I54 E66 S67 Y107 L212 L216
BS02 4NM B R20 Y32 K197 S198 L199 P200 R20 Y32 K197 S198 L199 P200
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016740 transferase activity
Biological Process
GO:0006749 glutathione metabolic 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:2vo4, PDBe:2vo4, PDBj:2vo4
PDBsum2vo4
PubMed19014949
UniProtO49235

[Back to BioLiP]