Structure of PDB 3qvp Chain A

Receptor sequence
>3qvpA (length=581) Species: 5061 (Aspergillus niger) [Search protein sequence]
GIEASLLTDPKDVSGRTVDYIIAGGGLTGLTTAARLTENPNISVLVIESG
SYESDRGPIIEDLNAYGDIFGSSVDHAYETVELATNNQTALIRSGNGLGG
STLVNGGTWTRPHKAQVDSWETVFGNEGWNWDNVAAYSLQAERARAPNAK
QIAAGHYFNASCHGVNGTVHAGPRDTGDDYSPIVKALMSAVEDRGVPTKK
DFGCGDPHGVSMFPNTLHEDQVRSDAAREWLLPNYQRPNLQVLTGQYVGK
VLLSQNGTTPRAVGVEFGTHKGNTHNVYAKHEVLLAAGSAVSPTILEYSG
IGMKSILEPLGIDTVVDLPVGLNLQDQTTATVRSRITSAGAGQGQAAWFA
TFNETFGDYSEKAHELLNTKLEQWAEEAVARGGFHNTTALLIQYENYRDW
IVNHNVAYSELFLDTAGVASFDVWDLLPFTRGYVHILDKDPYLHHFAYDP
QYFLNELDLLGQAAATQLARNISNSGAMQTYFAGETIPGDNLAYDADLSA
WTEYIPYHFRPNYHGVGTCSMMPKEMGGVVDNAARVYGVQGLRVIDGSIP
PTQMSSHVMTVFYAMALKISDAILEDYASMQ
3D structure
PDB3qvp Probing oxygen activation sites in two flavoprotein oxidases using chloride as an oxygen surrogate.
ChainA
Resolution1.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T357 W426 N514 H516 S558 H559
Catalytic site (residue number reindexed from 1) T355 W424 N512 H514 S556 H557
Enzyme Commision number 1.1.3.4: glucose oxidase.
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 FAD A G26 G28 L29 T30 E50 S51 H78 R95 G97 N98 G102 S103 N107 G108 T110 Y249 V250 A289 Y515 H559 V560 M561 F564 G24 G26 L27 T28 E48 S49 H76 R93 G95 N96 G100 S101 N105 G106 T108 Y247 V248 A287 Y513 H557 V558 M559 F562
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
View graph for
Cellular Component
External links
PDB RCSB:3qvp, PDBe:3qvp, PDBj:3qvp
PDBsum3qvp
PubMed21568312
UniProtP13006|GOX_ASPNG Glucose oxidase (Gene Name=gox)

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