2OQE
Crystal Structure of Hansenula polymorpha amine oxidase in complex with Xe to 1.6 Angstroms
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005777 | cellular_component | peroxisome |
| A | 0008131 | molecular_function | primary methylamine oxidase activity |
| A | 0009308 | biological_process | amine metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016641 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048038 | molecular_function | quinone binding |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005777 | cellular_component | peroxisome |
| B | 0008131 | molecular_function | primary methylamine oxidase activity |
| B | 0009308 | biological_process | amine metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016641 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048038 | molecular_function | quinone binding |
| C | 0005507 | molecular_function | copper ion binding |
| C | 0005777 | cellular_component | peroxisome |
| C | 0008131 | molecular_function | primary methylamine oxidase activity |
| C | 0009308 | biological_process | amine metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016641 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0048038 | molecular_function | quinone binding |
| D | 0005507 | molecular_function | copper ion binding |
| D | 0005777 | cellular_component | peroxisome |
| D | 0008131 | molecular_function | primary methylamine oxidase activity |
| D | 0009308 | biological_process | amine metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016641 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0048038 | molecular_function | quinone binding |
| E | 0005507 | molecular_function | copper ion binding |
| E | 0005777 | cellular_component | peroxisome |
| E | 0008131 | molecular_function | primary methylamine oxidase activity |
| E | 0009308 | biological_process | amine metabolic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016641 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0048038 | molecular_function | quinone binding |
| F | 0005507 | molecular_function | copper ion binding |
| F | 0005777 | cellular_component | peroxisome |
| F | 0008131 | molecular_function | primary methylamine oxidase activity |
| F | 0009308 | biological_process | amine metabolic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016641 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0048038 | molecular_function | quinone binding |
Functional Information from PROSITE/UniProt
| site_id | PS01159 |
| Number of Residues | 26 |
| Details | WW_DOMAIN_1 WW/rsp5/WWP domain signature. WgtgkrlqqalvYYrsdedd.SQYSHP |
| Chain | Residue | Details |
| C | TRP164-PRO189 | |
| A | TRP164-PRO189 |
| site_id | PS01164 |
| Number of Residues | 14 |
| Details | COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVVsqifTaaNYEY |
| Chain | Residue | Details |
| C | LEU394-TYR407 | |
| A | LEU394-TYR407 |
| site_id | PS01165 |
| Number of Residues | 14 |
| Details | COPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TfGitHFpapEDfP |
| Chain | Residue | Details |
| C | THR619-PRO632 | |
| A | THR619-PRO632 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Schiff-base intermediate with substrate; via topaquinone","evidences":[{"source":"PubMed","id":"10933787","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EKM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NBJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3T0U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KFF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 66 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"4EV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EV5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10933787","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A2V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EKM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OOV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3N9H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NBJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3T0U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EV5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KFD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KFE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KFF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q43077","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"2',4',5'-topaquinone","evidences":[{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A2V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"}]} |
| 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 | ASP319 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oac |
| Chain | Residue | Details |
| B | ASP319 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oac |
| Chain | Residue | Details |
| C | ASP319 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oac |
| Chain | Residue | Details |
| D | ASP319 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oac |
| Chain | Residue | Details |
| E | ASP319 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oac |
| Chain | Residue | Details |
| F | ASP319 |
