1IVW
Crystal structure of copper amine oxidase from Arthrobacter globiformis: Late intermediate in topaquinone biogenesis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005507 | molecular_function | copper ion binding |
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 |
A | 0052595 | molecular_function | aliphatic amine oxidase activity |
B | 0005507 | molecular_function | copper ion binding |
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 |
B | 0052595 | molecular_function | aliphatic amine oxidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU A 1001 |
Chain | Residue |
A | TPQ382 |
A | HIS431 |
A | HIS433 |
A | HIS592 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU B 1002 |
Chain | Residue |
B | TPQ382 |
B | HIS431 |
B | HIS433 |
B | HIS592 |
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 |
A | 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 |
A | THR587-PRO600 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P12807 |
Chain | Residue | Details |
A | ASP298 | |
B | ASP298 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0000250|UniProtKB:P12807 |
Chain | Residue | Details |
A | TPQ382 | |
B | TPQ382 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P12807 |
Chain | Residue | Details |
A | TYR296 | |
B | TYR296 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P46883 |
Chain | Residue | Details |
A | ILE379 | |
B | ILE379 |
Chain | Residue | Details |
A | HIS431 | |
A | HIS433 | |
A | HIS592 | |
B | HIS431 | |
B | HIS433 | |
B | HIS592 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:9405045 |
Chain | Residue | Details |
A | TPQ382 | |
B | TPQ382 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oac |
Chain | Residue | Details |
A | ASP298 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oac |
Chain | Residue | Details |
B | ASP298 |