Structure of PDB 4top Chain B

Receptor sequence
>4topB (length=219) Species: 3847 (Glycine max) [Search protein sequence]
MSDEVVLLDFWPSPFGMRVRIALAEKGIKYEYKEEDLRNKSPLLLQMNPV
HKKIPVLIHNGKPICESLIAVQYIEEVWNDRNPLLPSDPYQRAQTRFWAD
YVDKKIYDLGRKIWTSKGEEKEAAKKEFIEALKLLEEQLGDKTYFGGDNL
GFVDIALVPFYTWFKAYETFGTLNIESECPKFIAWAKRCLQKESVAKSLP
DQQKVYEFIMDLRKKLGIE
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.
ChainB
Resolution2.351 Å
3D
structure
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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 B S13 F15 L37 K40 K53 I54 E66 S67 S13 F15 L37 K40 K53 I54 E66 S67
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4top, PDBe:4top, PDBj:4top
PDBsum4top
PubMed
UniProtO49235

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