Structure of PDB 5agy Chain A

Receptor sequence
>5agyA (length=219) Species: 3847 (Glycine max) [Search protein sequence]
MQDEVVLLDFWPSPFGMRVRIALAEKGIKYEYKEEDLQNKSPLLLKMNPV
HKKIPVLIHNGKPICESLIAVQYIEEVWNDRNPLLPSDPYQRAQTRFWAD
YVDKKIYDLGRKICTSKGEEKEAAKKEFIEALKLLEEQLGDKTYFGGDNL
GFVDIALVPFYTWFKAYETFGTLNIESECPKFVAWAKRCLQKESVAKSLP
DQQKVYEFIMDLRKKLGIE
3D structure
PDB5agy Directed Evolution of Tau Class Glutathione Transferases Reveals a Site that Regulates Catalytic Efficiency and Masks Cooperativity.
ChainA
Resolution1.75 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 4NM A W11 R20 Y32 K197 L199 P200 W11 R20 Y32 K197 L199 P200
BS02 4NM A Y107 T115 W163 L212 Y107 T115 W163 L212
BS03 GTB A F10 S13 F15 L37 K40 K53 I54 E66 S67 Y107 F208 L212 F10 S13 F15 L37 K40 K53 I54 E66 S67 Y107 F208 L212
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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Cellular Component
External links
PDB RCSB:5agy, PDBe:5agy, PDBj:5agy
PDBsum5agy
PubMed26637269
UniProtI1MJ34

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