Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2HE3

Crystal structure of the selenocysteine to cysteine mutant of human glutathionine peroxidase 2 (GPX2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0004602molecular_functionglutathione peroxidase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006979biological_processresponse to oxidative stress
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0045171cellular_componentintercellular bridge
A0047066molecular_functionphospholipid-hydroperoxide glutathione peroxidase activity
A0072686cellular_componentmitotic spindle
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 189
ChainResidue
APHE57
APRO58
AARG59
AARG60

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 190
ChainResidue
AGLY160
AGLU162
AGLY163
AGLU164

Functional Information from PROSITE/UniProt
site_idPS00460
Number of Residues16
DetailsGLUTATHIONE_PEROXID_1 Glutathione peroxidases active site. GRaVLIeNVaSlCGtT
ChainResidueDetails
AGLY28-THR43

site_idPS00763
Number of Residues8
DetailsGLUTATHIONE_PEROXID_2 Glutathione peroxidases signature 2. LGFPCNQF
ChainResidueDetails
ALEU64-PHE71

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:O70325
ChainResidueDetails
ACYS40

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gp1
ChainResidueDetails
ATRP152
AGLN74

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon