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

1GPE

GLUCOSE OXIDASE FROM PENICILLIUM AMAGASAKIENSE

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0046562molecular_functionbeta-D-glucose oxidase activity
A0050660molecular_functionflavin adenine dinucleotide binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0016491molecular_functionoxidoreductase activity
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0046562molecular_functionbeta-D-glucose oxidase activity
B0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. TAAQLAAGHSF
ChainResidueDetails
ATHR154-PHE164

site_idPS00623
Number of Residues24
DetailsGMC_OXRED_1 GMC oxidoreductases signature 1. GKgLGGSTlINgdsWtrPdkvqiD
ChainResidueDetails
AGLY101-ASP124

site_idPS00624
Number of Residues15
DetailsGMC_OXRED_2 GMC oxidoreductases signature 2. GSaiSPlILeySGIG
ChainResidueDetails
AGLY294-GLY308

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P13006","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1GPE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"1GPE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1gal
ChainResidueDetails
AGLU416
AHIS520
AHIS563

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1gal
ChainResidueDetails
BGLU416
BHIS520
BHIS563

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gal
ChainResidueDetails
AHIS520
AHIS563

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gal
ChainResidueDetails
BHIS520
BHIS563

242842

PDB entries from 2025-10-08

PDB statisticsPDBj update infoContact PDBjnumon