Structure of PDB 2vo4 Chain B Binding Site BS02

Receptor Information

>2vo4 Chain B (length=219) Species: 3847 (Glycine max)

MQDEVVLLDFWPSPFGMRVRIALAEKGIKYEYKEEDLRNKSPLLLQMNPV
HKKIPVLIHNGKPICESLIAVQYIEEVWNDRNPLLPSDPYQRAQTRFWAD
YVDKKIYDLGRKIWTSKGEEKEAAKKEFIEALKLLEEQLGDKTYFGGDNL
GFVDIALVPFYTWFKAYETFGTLNIESECPKFIAWAKRCLQKESVAKSLP
DQQKVYEFIMDLRKKLGIE

Ligand information

• Ligand ID: 4NM
• InChI: InChI=1S/C7H7NO2S/c9-8(10)7-3-1-6(5-11)2-4-7/h1-4H,5H2,(H-,9,10,11)/p+1
• InChIKey: OTHKGVFNUSHUQO-UHFFFAOYSA-O
• SMILES:
  ACDLabs 10.04: O=[N+](O)c1ccc(cc1)CS
  OpenEye OEToolkits 1.5.0: c1cc(ccc1CS)[N+](=O)O
  CACTVS 3.341: O[N+](=O)c1ccc(CS)cc1
• Formula: C7 H8 N O2 S
• Name: 4-NITROPHENYL METHANETHIOL
• PDB chain: 2vo4 Chain B Residue 1221

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2vo4 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.
• Resolution: 1.75 Å
• Binding residue (original residue number in PDB): R20 Y32 K197 S198 L199 P200
• Binding residue (residue number reindexed from 1): R20 Y32 K197 S198 L199 P200
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 2.5.1.18: glutathione transferase.

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

External links

• PDB: RCSB:2vo4, PDBe:2vo4, PDBj:2vo4
• PDBsum: 2vo4
• PubMed: 19014949
• UniProt: O49235