Structure of PDB 4yh2 Chain A

Receptor sequence
>4yh2A (length=221) Species: 7227 (Drosophila melanogaster) [Search protein sequence]
VKLTLYGLDPSPPVRAVKLTLAALNLTYEYVNVDIVARAQLSPEYLEKNP
QHTVPTLEDDGHYIWDSHAIIAYLVSKYADSDALYPKDPLKRAVVDQRLH
FESGVVFANGIRSISKSVLFQGQTKVPKERYDAIIEIYDFVETFLKGQDY
IAGNQLTIADFSLVSSVASLEAFVALDTTKYPRIGAWIKKLEQLPYYEEA
NGKGVRQLVAIFKKTNFTFEA
3D structure
PDB4yh2 Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site
ChainA
Resolution1.72 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S12
Catalytic site (residue number reindexed from 1) S11
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 GSH A S12 P14 Q41 H53 T54 V55 D67 S68 H69 F108 R113 S11 P13 Q40 H52 T53 V54 D66 S67 H68 F107 R112
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004364 glutathione transferase activity
GO:0004602 glutathione peroxidase activity
GO:0005515 protein binding
GO:0016740 transferase activity
Biological Process
GO:0006749 glutathione metabolic process
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:4yh2, PDBe:4yh2, PDBj:4yh2
PDBsum4yh2
PubMed26487708
UniProtA1ZB71

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