Structure of PDB 4png Chain A

Receptor sequence
>4pngA (length=221) Species: 7227 (Drosophila melanogaster) [Search protein sequence]
KLILYGLEASPPVRAVKLTLAALEVPYEFVEVNTRAKENFSEEFLKKNPQ
HTVPTLEDDGHYIWDSHAIIAYLVSKYGKTDSLYPKDLLQRAVVDQRLHF
ESGVIFANALRSITKPLFAGKQTMIPKERYDAIIEVYDFLEKFLAGNDYV
AGNQLTIADFSIISTVSSLEVFVKVDTTKYPRIAAWFKRLQKLPYYEEAN
GNGARTFESFIREYNFTFASN
3D structure
PDB4png Comparison of epsilon- and delta-class glutathione S-transferases: the crystal structures of the glutathione S-transferases DmGSTE6 and DmGSTE7 from Drosophila melanogaster.
ChainA
Resolution1.53 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) S10
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 GSF A S12 P14 T36 N41 H53 T54 V55 D67 S68 H69 F108 S10 P12 T34 N39 H51 T52 V53 D65 S66 H67 F106
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:4png, PDBe:4png, PDBj:4png
PDBsum4png
PubMed26457432
UniProtA1ZB72

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