Structure of PDB 1gpe Chain A

Receptor sequence
>1gpeA (length=587) Species: 63559 (Penicillium amagasakiense) [Search protein sequence]
YLPAQQIDVQSSLLSDPSKVAGKTYDYIIAGGGLTGLTVAAKLTENPKIK
VLVIEKGFYESNDGAIIEDPNAYGQIFGTTVDQNYLTVPLINNRTNNIKA
GKGLGGSTLINGDSWTRPDKVQIDSWEKVFGMEGWNWDNMFEYMKKAEAA
RTPTAAQLAAGHSFNATCHGTNGTVQSGARDNGQPWSPIMKALMNTVSAL
GVPVQQDFLCGHPRGVSMIMNNLDENQVRVDAARAWLLPNYQRSNLEILT
GQMVGKVLFKQTASGPQAVGVNFGTNKAVNFDVFAKHEVLLAAGSAISPL
ILEYSGIGLKSVLDQANVTQLLDLPVGINMQDQTTTTVSSRASSAGAGQG
QAVFFANFTETFGDYAPQARDLLNTKLDQWAEETVARGGFHNVTALKVQY
ENYRNWLLDEDVAFAELFMDTEGKINFDLWDLIPFTRGSVHILSSDPYLW
QFANDPKFFLNEFDLLGQAAASKLARDLTSQGAMKEYFAGETLPGYNLVQ
NATLSQWSDYVLQNFRPNWHAVSSCSMMSRELGGVVDATAKVYGTQGLRV
IDGSIPPTQVSSHVMTIFYGMALKVADAILDDYAKSA
3D structure
PDB1gpe 1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T361 W430 N518 H520 S562 H563
Catalytic site (residue number reindexed from 1) T361 W430 N518 H520 S562 H563
Enzyme Commision number 1.1.3.4: glucose oxidase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016614 oxidoreductase activity, acting on CH-OH group of donors
GO:0046562 glucose oxidase activity
GO:0050660 flavin adenine dinucleotide binding
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Cellular Component
External links
PDB RCSB:1gpe, PDBe:1gpe, PDBj:1gpe
PDBsum1gpe
PubMed10216293
UniProtP81156|GOX_PENAG Glucose oxidase

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