Structure of PDB 5agy Chain A Binding Site BS01

Receptor Information

>5agy Chain A (length=219) Species: 3847 (Glycine max)

MQDEVVLLDFWPSPFGMRVRIALAEKGIKYEYKEEDLQNKSPLLLKMNPV
HKKIPVLIHNGKPICESLIAVQYIEEVWNDRNPLLPSDPYQRAQTRFWAD
YVDKKIYDLGRKICTSKGEEKEAAKKEFIEALKLLEEQLGDKTYFGGDNL
GFVDIALVPFYTWFKAYETFGTLNIESECPKFVAWAKRCLQKESVAKSLP
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: 5agy Chain A Residue 1220

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5agy Directed Evolution of Tau Class Glutathione Transferases Reveals a Site that Regulates Catalytic Efficiency and Masks Cooperativity.
• Resolution: 1.75 Å
• Binding residue (original residue number in PDB): W11 R20 Y32 K197 L199 P200
• Binding residue (residue number reindexed from 1): W11 R20 Y32 K197 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:5agy, PDBe:5agy, PDBj:5agy
• PDBsum: 5agy
• PubMed: 26637269
• UniProt: I1MJ34