6L9C
Neutron structure of copper amine oxidase from Arthrobacter glibiformis at pD 7.4
Functional Information from GO Data
Chain | GOid | namespace | contents |
X | 0005507 | molecular_function | copper ion binding |
X | 0008131 | molecular_function | primary methylamine oxidase activity |
X | 0009308 | biological_process | amine metabolic process |
X | 0016491 | molecular_function | oxidoreductase activity |
X | 0016641 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor |
X | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue CU X 701 |
Chain | Residue |
X | HIS431 |
X | HIS433 |
X | HIS592 |
X | HOH1031 |
X | HOH1415 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue NA X 702 |
Chain | Residue |
X | HOH1185 |
X | ASP440 |
X | MET441 |
X | ASP581 |
X | ILE582 |
site_id | AC3 |
Number of Residues | 15 |
Details | binding site for Ligand residues TPQ X 382 through ASP X 383 bound to ASN X 381 |
Chain | Residue |
X | VAL282 |
X | TYR284 |
X | TYR296 |
X | ASA298 |
X | THR377 |
X | THR378 |
X | ILE379 |
X | GLY380 |
X | ASN381 |
X | TYR384 |
X | THR403 |
X | GLY404 |
X | HIS433 |
X | HOH1239 |
X | HOH1415 |
Functional Information from PROSITE/UniProt
site_id | PS01164 |
Number of Residues | 14 |
Details | COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. MVIsfftTigNYDY |
Chain | Residue | Details |
X | MET371-TYR384 |
site_id | PS01165 |
Number of Residues | 14 |
Details | COPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TfGltHFprvEDwP |
Chain | Residue | Details |
X | THR587-PRO600 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P12807 |
Chain | Residue | Details |
X | ASA298 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0000250|UniProtKB:P12807 |
Chain | Residue | Details |
X | E9C382 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P12807 |
Chain | Residue | Details |
X | TYR296 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P46883 |
Chain | Residue | Details |
X | ILE379 |
Chain | Residue | Details |
X | HIS431 | |
X | HIS433 | |
X | HIS592 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:9405045 |
Chain | Residue | Details |
X | E9C382 |