3KPF
X-ray structure of the mutant Lys300Met of polyamine oxidase from Zea mays
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006598 | biological_process | polyamine catabolic process |
| A | 0009505 | cellular_component | plant-type cell wall |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046208 | biological_process | spermine catabolic process |
| A | 0046592 | molecular_function | polyamine oxidase activity |
| A | 0048046 | cellular_component | apoplast |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0052897 | molecular_function | N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity |
| A | 0052900 | molecular_function | spermine oxidase (propane-1,3-diamine-forming) activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006598 | biological_process | polyamine catabolic process |
| B | 0009505 | cellular_component | plant-type cell wall |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046208 | biological_process | spermine catabolic process |
| B | 0046592 | molecular_function | polyamine oxidase activity |
| B | 0048046 | cellular_component | apoplast |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0052897 | molecular_function | N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity |
| B | 0052900 | molecular_function | spermine oxidase (propane-1,3-diamine-forming) activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Glycosylation: {"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"}]} |
| Chain | Residue | Details |
