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1H86

COVALENT ADDUCT BETWEEN POLYAMINE OXIDASE AND N1ethylN11((cycloheptyl)methyl)4,8diazaundecane at pH 7.0

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0006598biological_processpolyamine catabolic process
A0009505cellular_componentplant-type cell wall
A0016491molecular_functionoxidoreductase activity
A0046208biological_processspermine catabolic process
A0046592molecular_functionpolyamine oxidase activity
A0048046cellular_componentapoplast
A0050660molecular_functionflavin adenine dinucleotide binding
A0052897molecular_functionN8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity
A0052900molecular_functionspermine oxidase (propane-1,3-diamine-forming) activity
B0005576cellular_componentextracellular region
B0006598biological_processpolyamine catabolic process
B0009505cellular_componentplant-type cell wall
B0016491molecular_functionoxidoreductase activity
B0046208biological_processspermine catabolic process
B0046592molecular_functionpolyamine oxidase activity
B0048046cellular_componentapoplast
B0050660molecular_functionflavin adenine dinucleotide binding
B0052897molecular_functionN8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity
B0052900molecular_functionspermine oxidase (propane-1,3-diamine-forming) activity
C0005576cellular_componentextracellular region
C0006598biological_processpolyamine catabolic process
C0009505cellular_componentplant-type cell wall
C0016491molecular_functionoxidoreductase activity
C0046208biological_processspermine catabolic process
C0046592molecular_functionpolyamine oxidase activity
C0048046cellular_componentapoplast
C0050660molecular_functionflavin adenine dinucleotide binding
C0052897molecular_functionN8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity
C0052900molecular_functionspermine oxidase (propane-1,3-diamine-forming) activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10368296","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11258887","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1B5Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1H82","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2009","submissionDatabase":"PDB data bank","title":"The crystal structure of the mutant Lys300Met of polyamine oxidase from Zea Mays unveils the role of Lys300 in catalysis.","authors":["Fiorillo A.","Ilari A.","Tavladoraki P."]}},{"source":"PDB","id":"3KU9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L1R","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10368296","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11258887","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1B5Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1H82","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b5q
ChainResidueDetails
AGLU62

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b5q
ChainResidueDetails
BGLU62

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b5q
ChainResidueDetails
CGLU62

site_idMCSA1
Number of Residues1
DetailsM-CSA 809
ChainResidueDetails
AGLU62proton acceptor, proton donor

site_idMCSA2
Number of Residues1
DetailsM-CSA 809
ChainResidueDetails
BGLU62proton acceptor, proton donor

site_idMCSA3
Number of Residues1
DetailsM-CSA 809
ChainResidueDetails
CGLU62proton acceptor, proton donor

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PDB entries from 2025-07-30

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