Structure of PDB 3q19 Chain A

Receptor sequence

>3q19A (length=224) Species: 9606 (Homo sapiens)

ATRTLGKGSQPPGPVPEGLIRIYSMRFCPYSHRTRLVLKAKDIRHEVVNI
NLRNKPEWYYTKHPFGHIPVLETSQSQLIYESVIACEYLDDAYPGRKLFP
YDPYERARQKMLLELFSKVPHLTKECLVALRSGRESTNLKAALRQEFSNL
EEILEYQNTTFFGGTSISMIDYLLWPWFERLDVYGILDCVSHTPALRLWI
SAMKWDPTVSALLMDKSIFQGFLN

3D structure

• PDB: 3q19 Structural insights into the dehydroascorbate reductase activity of human omega-class glutathione transferases.
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Enzyme Commision number: 1.20.4.2: methylarsonate reductase.
  1.8.5.1: glutathione dehydrogenase (ascorbate).
  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	C32 Y34 K59 H71 I72 E85 S86	C28 Y30 K55 H67 I68 E81 S82

Gene Ontology

Molecular Function

• GO:0004364 glutathione transferase activity
• GO:0005515 protein binding
• GO:0016491 oxidoreductase activity
• GO:0016740 transferase activity
• GO:0042802 identical protein binding
• GO:0045174 glutathione dehydrogenase (ascorbate) activity
• GO:0050610 methylarsonate reductase activity

Biological Process

• GO:0006749 glutathione metabolic process
• GO:0006805 xenobiotic metabolic process
• GO:0019852 L-ascorbic acid metabolic process
• GO:0071243 cellular response to arsenic-containing substance
• GO:0098869 cellular oxidant detoxification

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0070062 extracellular exosome

External links

• PDB: RCSB:3q19, PDBe:3q19, PDBj:3q19
• PDBsum: 3q19
• PubMed: 22522127
• UniProt: Q9H4Y5|GSTO2_HUMAN Glutathione S-transferase omega-2 (Gene Name=GSTO2)