Structure of PDB 1b5q Chain B

Receptor sequence
>1b5qB (length=462) Species: 4577 (Zea mays) [Search protein sequence]
PRVIVVGAGMSGISAAKRLSEAGITDLLILEATDHIGGRMHKTNFAGINV
ELGANWVEGVNGGKMNPIWPIVNSTLKLRNFRSDFDYLAQNVYKEDGGVY
DEDYVQKRIELADSVEEMGEKLSATLHASGRDDMSILAMQRLNEHQPNGP
ATPVDMVVDYYKFDYEFAEPPRVTSLQNTVPLATFSDFGDDVYFVADQRG
YEAVVYYLAGQYLKTDDKSGKIVDPRLQLNKVVREIKYSPGGVTVKTEDN
SVYSADYVMVSASLGVLQSDLIQFKPKLPTWKVRAIYQFDMAVYTKIFLK
FPRKFWPEGKGREFFLYASSRRGYYGVWQEFEKQYPDANVLLVTVTDEES
RRIEQQSDEQTKAEIMQVLRKMFPGKDVPDATDILVPRWWSDRFYKGTFS
NWPVGVNRYEYDQLRAPVGRVYFTGEHTSEHYNGYVHGAYLSGIDSAEIL
INCAQKKMCKYH
3D structure
PDB1b5q A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase.
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E62 D195 K300
Catalytic site (residue number reindexed from 1) E58 D191 K296
Enzyme Commision number 1.5.3.14: polyamine oxidase (propane-1,3-diamine-forming).
1.5.3.15: N(8)-acetylspermidine oxidase (propane-1,3-diamine-forming).
Interaction with ligand
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0046592 polyamine oxidase activity
GO:0050660 flavin adenine dinucleotide binding
GO:0052897 N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity
GO:0052900 spermine oxidase (propane-1,3-diamine-forming) activity
Biological Process
GO:0006598 polyamine catabolic process
GO:0046208 spermine catabolic process
Cellular Component
GO:0009505 plant-type cell wall
GO:0048046 apoplast

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1b5q, PDBe:1b5q, PDBj:1b5q
PDBsum1b5q
PubMed10368296
UniProtO64411|PAO1_MAIZE Polyamine oxidase 1 (Gene Name=MPAO1)

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