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3QAG

Human Glutathione Transferase O2 with glutathione -new crystal form

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006749biological_processglutathione metabolic process
A0006805biological_processxenobiotic metabolic process
A0016491molecular_functionoxidoreductase activity
A0016740molecular_functiontransferase activity
A0019852biological_processL-ascorbic acid metabolic process
A0042802molecular_functionidentical protein binding
A0045174molecular_functionglutathione dehydrogenase (ascorbate) activity
A0050610molecular_functionmethylarsonate reductase activity
A0055114biological_processobsolete oxidation-reduction process
A0070062cellular_componentextracellular exosome
A0071243biological_processcellular response to arsenic-containing substance
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GSH A 1001
ChainResidue
ACYS32
AHOH308
AHOH327
ATYR34
ALYS59
AHIS71
AILE72
APRO73
AGLU85
ASER86
AHOH249

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 1002
ChainResidue
ALYS101
ALEU102
APHE103
AGLY167
ASER172

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PEG A 1003
ChainResidue
ATRP209

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ACYS32

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:22522127
ChainResidueDetails
ALYS59
AILE72
AGLU85

222415

PDB entries from 2024-07-10

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