3HII
Crystal structure of human diamine oxidase in complex with the inhibitor pentamidine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005923 | cellular_component | bicellular tight junction |
| A | 0008131 | molecular_function | primary methylamine oxidase activity |
| A | 0008201 | molecular_function | heparin binding |
| A | 0009308 | biological_process | amine metabolic process |
| A | 0009445 | biological_process | putrescine metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0035580 | cellular_component | specific granule lumen |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048038 | molecular_function | quinone binding |
| A | 0050232 | molecular_function | putrescine oxidase activity |
| A | 0052597 | molecular_function | diamine oxidase activity |
| A | 0052598 | molecular_function | histamine oxidase activity |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005923 | cellular_component | bicellular tight junction |
| B | 0008131 | molecular_function | primary methylamine oxidase activity |
| B | 0008201 | molecular_function | heparin binding |
| B | 0009308 | biological_process | amine metabolic process |
| B | 0009445 | biological_process | putrescine metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0035580 | cellular_component | specific granule lumen |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048038 | molecular_function | quinone binding |
| B | 0050232 | molecular_function | putrescine oxidase activity |
| B | 0052597 | molecular_function | diamine oxidase activity |
| B | 0052598 | molecular_function | histamine oxidase activity |
| B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PROSITE/UniProt
| site_id | PS01164 |
| Number of Residues | 14 |
| Details | COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVLrttsTvyNYDY |
| Chain | Residue | Details |
| A | LEU450-TYR463 |
| site_id | PS01165 |
| Number of Residues | 14 |
| Details | COPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TvGflHIphsEDiP |
| Chain | Residue | Details |
| A | THR670-PRO683 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"19764817","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Schiff-base intermediate with substrate; via topaquinone","evidences":[{"source":"PubMed","id":"19764817","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HI7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HIG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HII","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K5T","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19764817","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HI7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HIG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HII","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K5T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MPH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"2',4',5'-topaquinone","evidences":[{"source":"PubMed","id":"19764817","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19764817","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HI7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HIG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HII","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K5T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MPH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oac |
| Chain | Residue | Details |
| A | ASP373 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oac |
| Chain | Residue | Details |
| B | ASP373 |
