Structure of PDB 5agy Chain B

Receptor sequence
>5agyB (length=217) Species: 3847 (Glycine max) [Search protein sequence]
DEVVLLDFWPSPFGMRVRIALAEKGIKYEYKEEDLQNKSPLLLKMNPVHK
KIPVLIHNGKPICESLIAVQYIEEVWNDRNPLLPSDPYQRAQTRFWADYV
DKKIYDLGRKICTSKGEEKEAAKKEFIEALKLLEEQLGDKTYFGGDNLGF
VDIALVPFYTWFKAYETFGTLNIESECPKFVAWAKRCLQKESVAKSLPDQ
QKVYEFIMDLRKKLGIE
3D structure
PDB5agy Directed Evolution of Tau Class Glutathione Transferases Reveals a Site that Regulates Catalytic Efficiency and Masks Cooperativity.
ChainB
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 GTB B S13 F15 L37 K40 K53 I54 E66 S67 Y107 F208 L212 S11 F13 L35 K38 K51 I52 E64 S65 Y105 F206 L210
BS02 4NM B Y107 R111 I209 L212 Y105 R109 I207 L210
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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