Structure of PDB 5agy Chain A Binding Site BS02

Receptor Information
>5agy Chain A (length=219) Species: 3847 (Glycine max) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MQDEVVLLDFWPSPFGMRVRIALAEKGIKYEYKEEDLQNKSPLLLKMNPV
HKKIPVLIHNGKPICESLIAVQYIEEVWNDRNPLLPSDPYQRAQTRFWAD
YVDKKIYDLGRKICTSKGEEKEAAKKEFIEALKLLEEQLGDKTYFGGDNL
GFVDIALVPFYTWFKAYETFGTLNIESECPKFVAWAKRCLQKESVAKSLP
DQQKVYEFIMDLRKKLGIE
Ligand information
Ligand ID4NM
InChIInChI=1S/C7H7NO2S/c9-8(10)7-3-1-6(5-11)2-4-7/h1-4H,5H2,(H-,9,10,11)/p+1
InChIKeyOTHKGVFNUSHUQO-UHFFFAOYSA-O
SMILES
SoftwareSMILES
ACDLabs 10.04O=[N+](O)c1ccc(cc1)CS
OpenEye OEToolkits 1.5.0c1cc(ccc1CS)[N+](=O)O
CACTVS 3.341O[N+](=O)c1ccc(CS)cc1
FormulaC7 H8 N O2 S
Name4-NITROPHENYL METHANETHIOL
ChEMBL
DrugBank
ZINC
PDB chain5agy Chain A Residue 1221 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5agy Directed Evolution of Tau Class Glutathione Transferases Reveals a Site that Regulates Catalytic Efficiency and Masks Cooperativity.
Resolution1.75 Å
Binding residue
(original residue number in PDB)
Y107 T115 W163 L212
Binding residue
(residue number reindexed from 1)
Y107 T115 W163 L212
Annotation score1
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5agy, PDBe:5agy, PDBj:5agy
PDBsum5agy
PubMed26637269
UniProtI1MJ34

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