Structure of PDB 4top Chain A

Receptor sequence
>4topA (length=218) Species: 3847 (Glycine max) [Search protein sequence]
SDEVVLLDFWPSPFGMRVRIALAEKGIKYEYKEEDLRNKSPLLLQMNPVH
KKIPVLIHNGKPICESLIAVQYIEEVWNDRNPLLPSDPYQRAQTRFWADY
VDKKIYDLGRKIWTSKGEEKEAAKKEFIEALKLLEEQLGDKTYFGGDNLG
FVDIALVPFYTWFKAYETFGTLNIESECPKFIAWAKRCLQKESVAKSLPD
QQKVYEFIMDLRKKLGIE
3D structure
PDB4top Crystal structure of Glycine max glutathione transferase in complex with glutathione: investigation of the mechanism operating by the Tau class glutathione transferases.
ChainA
Resolution2.351 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 GSH A S13 F15 L37 K40 K53 I54 E66 S67 S12 F14 L36 K39 K52 I53 E65 S66
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:4top, PDBe:4top, PDBj:4top
PDBsum4top
PubMed
UniProtO49235

[Back to BioLiP]