3SX1
Hansenula polymorpha copper amine oxidase-1 in its apo form
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 693 |
| Chain | Residue |
| C | HIS23 |
| C | TYR64 |
| C | LYS68 |
| C | LYS265 |
| C | ASP280 |
| C | HOH989 |
| C | HOH1975 |
| C | HOH2352 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 693 |
| Chain | Residue |
| A | LYS219 |
| A | TYR448 |
| A | TYR534 |
| A | HIS218 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 693 |
| Chain | Residue |
| B | HIS23 |
| B | TYR64 |
| B | LYS68 |
| B | LYS265 |
| B | ASP280 |
| B | HOH724 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 694 |
| Chain | Residue |
| B | ARG163 |
| B | PHE310 |
| B | HOH917 |
| B | HOH1248 |
| B | HOH2873 |
| C | HOH765 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 694 |
| Chain | Residue |
| A | PRO442 |
| A | PRO484 |
| A | TYR485 |
| A | HOH852 |
| A | HOH2150 |
| A | HOH2814 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 694 |
| Chain | Residue |
| C | ARG213 |
| C | LYS214 |
| C | VAL215 |
| C | GLY435 |
| C | ASP436 |
| C | ASN450 |
| C | HOH836 |
| C | HOH1101 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 695 |
| Chain | Residue |
| A | ARG211 |
| A | LYS214 |
| A | VAL215 |
| A | GLY435 |
| A | ASP436 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 695 |
| Chain | Residue |
| A | GLN70 |
| B | HIS218 |
| B | LYS219 |
| B | TYR448 |
| B | PRO449 |
| B | HOH1040 |
| C | TYR534 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 696 |
| Chain | Residue |
| A | GLN66 |
| A | GLN70 |
| A | GLY72 |
| A | HOH2485 |
| C | TYR534 |
| C | THR650 |
| C | HOH750 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 696 |
| Chain | Residue |
| B | PRO484 |
| B | TYR485 |
| B | TYR499 |
| B | HOH1622 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL C 695 |
| Chain | Residue |
| C | PRO484 |
| C | TYR485 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 C 696 |
| Chain | Residue |
| C | ARG20 |
| C | HIS218 |
| C | LYS219 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 697 |
| Chain | Residue |
| B | PRO442 |
| B | HOH2980 |
| C | PRO484 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 697 |
| Chain | Residue |
| A | TRP67 |
| A | LYS68 |
| A | HOH2024 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 698 |
| Chain | Residue |
| A | GLY142 |
| A | GLU147 |
| A | TYR177 |
| A | HOH792 |
| A | HOH908 |
| B | HOH2841 |
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 |
| A | TRP164-PRO189 |
| site_id | PS01164 |
| Number of Residues | 14 |
| Details | COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVVsqifTaaNYEY |
| Chain | Residue | Details |
| 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 |
| A | THR619-PRO632 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| 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 | 3 |
| 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 | 33 |
| 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 | 15 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P46883","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 9 |
| 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_FI6 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q43077","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| 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_FI8 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






