Structure of PDB 5niw Chain A

Receptor sequence
>5niwA (length=578) Species: 5061 (Aspergillus niger) [Search protein sequence]
GIEASLLTDPKDVSGRTVDYIIAGGGLVGLTTAAKLTENPNISVLVIESG
SYESDRGPIIEDLNAYGDIFGSSVDHAYETVELATNNQTALVRSGNGLGG
STLINGGTWTRPHKAQVDSWETVFGNEGWNWDNVAAYSLQAERARAPNAK
QIAAGHYFNTSCHGVNGTVHAGPRDTGDDYSPIVKALMSAVEDRGVPTKK
DFGCGDPHGVSMFPNTLHEDQVRSDAAREWLLPNYQRPNLQVLTGQYVGK
VLLSQNGTTPRAVGVEFGTHKGNTHNVYAKHEVLLAAGSAVSPTILEYSG
IGMKSILEPLGIDTVVDLPVGLNLQDQTTATVRSRITSAGAGQGQAAWFA
TFNETFGDYSEKAHELLNTKLQWAEEAVARGGFHNTTALLIQYENYRDWI
VNHNVAYSELFLDTAGVASFDVWDLLPFTRGYVHILDKDPYLHHFAYDPQ
YFLNELDLLGQAAATQLARNISNSGAMQTYFAGETIPGDNLAYDADLSAW
TEYIPYHFRPNYHGVGTCSMMPKEMGGVVDNAARVYGVQGLRVIDGSIPP
TQVSSHVMTVFYAMALKISDAILEDYAS
3D structure
PDB5niw Shuffling Active Site Substate Populations Affects Catalytic Activity: The Case of Glucose Oxidase.
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) T357 W426 N514 H516 S558 H559
Catalytic site (residue number reindexed from 1) T355 W423 N511 H513 S555 H556
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 V30 I49 E50 S51 H78 R95 G97 N98 G102 S103 N107 G108 T110 Y249 V250 A289 Y515 H559 V560 M561 F564 G24 G26 L27 V28 I47 E48 S49 H76 R93 G95 N96 G100 S101 N105 G106 T108 Y247 V248 A287 Y512 H556 V557 M558 F561
BS02 OXY A H516 H559 V560 H513 H556 V557
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:5niw, PDBe:5niw, PDBj:5niw
PDBsum5niw
PubMed29291138
UniProtP13006|GOX_ASPNG Glucose oxidase (Gene Name=gox)

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