3T0U
Hansenula polymorpha copper amine oxidase-1 in complex with Cu(I)
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 | 5 |
Details | BINDING SITE FOR RESIDUE CU1 A 801 |
Chain | Residue |
A | TYR405 |
A | LEU425 |
A | HIS456 |
A | HIS458 |
A | HIS624 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 802 |
Chain | Residue |
A | ASP280 |
A | HOH1162 |
A | HIS23 |
A | TYR64 |
A | LYS68 |
A | LYS265 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 803 |
Chain | Residue |
A | PRO484 |
A | TYR485 |
A | TYR499 |
A | HOH1413 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 804 |
Chain | Residue |
A | TRP67 |
A | LYS68 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 805 |
Chain | Residue |
A | LYS393 |
A | ARG420 |
A | ASP422 |
A | ARG424 |
A | HOH969 |
A | HOH1158 |
A | HOH1300 |
A | HOH1516 |
B | GLY371 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 806 |
Chain | Residue |
A | LYS561 |
A | LYS561 |
A | SER591 |
A | ASP593 |
A | HOH1241 |
A | HOH1241 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU1 B 801 |
Chain | Residue |
B | TYR405 |
B | LEU425 |
B | HIS456 |
B | HIS458 |
B | HIS624 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 802 |
Chain | Residue |
B | TYR534 |
B | HOH1001 |
B | HOH1461 |
C | GLN66 |
C | GLN70 |
C | GLY72 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 803 |
Chain | Residue |
B | HIS23 |
B | TYR64 |
B | LYS68 |
B | LYS265 |
B | ASP280 |
B | HOH1065 |
B | HOH1692 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PO4 B 804 |
Chain | Residue |
B | HIS218 |
B | LYS219 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE GOL B 805 |
Chain | Residue |
C | TRP67 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 806 |
Chain | Residue |
B | LYS214 |
B | VAL215 |
B | ASP436 |
B | HOH1307 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 807 |
Chain | Residue |
A | PRO442 |
B | PRO484 |
B | TYR485 |
B | HOH1371 |
B | HOH1424 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 808 |
Chain | Residue |
B | LYS561 |
B | SER591 |
B | HOH1392 |
C | LYS561 |
C | ASP593 |
C | GOL805 |
C | HOH1022 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU1 C 801 |
Chain | Residue |
C | TYR405 |
C | HIS456 |
C | HIS458 |
C | HIS624 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 802 |
Chain | Residue |
C | PRO442 |
C | PRO484 |
C | TYR485 |
C | HOH1424 |
C | HOH1656 |
site_id | BC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL C 803 |
Chain | Residue |
A | HOH1432 |
C | ARG61 |
C | LYS62 |
C | GLN70 |
C | ASP471 |
C | ASP613 |
C | HOH1648 |
C | HOH1783 |
C | HOH1798 |
site_id | BC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL C 804 |
Chain | Residue |
C | GLY371 |
C | LYS393 |
C | VAL412 |
C | ASP422 |
C | ARG424 |
C | HOH923 |
C | HOH1110 |
C | HOH1765 |
site_id | CC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 805 |
Chain | Residue |
C | SER591 |
C | HOH1022 |
C | HOH1333 |
B | LYS561 |
B | ASP593 |
B | GOL808 |
C | LYS561 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL C 806 |
Chain | Residue |
C | HIS23 |
C | TYR64 |
C | LYS68 |
C | LYS265 |
C | ASP280 |
C | HOH1092 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL C 807 |
Chain | Residue |
C | HIS218 |
C | LYS219 |
C | TYR448 |
C | TYR534 |
site_id | CC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL C 808 |
Chain | Residue |
C | LYS214 |
C | VAL215 |
C | GLY435 |
C | ASP436 |
site_id | CC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 809 |
Chain | Residue |
C | GLY142 |
C | PRO144 |
C | GLU147 |
C | TYR177 |
C | HOH1258 |
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 |