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 |
| A | 0052597 | molecular_function | diamine 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 |
| B | 0052597 | molecular_function | diamine oxidase activity |
Functional Information from PDB Data
| site_id | ACA |
| Number of Residues | 7 |
| Details | THE COPPER ATOM IN THE ACTIVE SITE OF EACH SUBUNIT IS LIGATED TO THREE HISTIDINE RESIDUES AND TWO WATER MOLECULES IN A DISTORTED SQUARE PYRAMIDAL ARRANGEMENT. THE ORGANIC COFACTOR TOPA QUINONE (TPQ) IS IN THE ACTIVE SITE WITH THE NEAREST QUINONE OXYGEN ATOM AT ~6A FROM THE COPPER ATOM. |
| Chain | Residue |
| A | HIS442 |
| A | HIS444 |
| A | HIS603 |
| A | CU650 |
| A | HOH658 |
| A | HOH659 |
| A | TPQ387 |
| site_id | ACB |
| Number of Residues | 7 |
| Details | THE COPPER ATOM IN THE ACTIVE SITE OF EACH SUBUNIT IS LIGATED TO THREE HISTIDINE RESIDUES AND TWO WATER MOLECULES IN A DISTORTED SQUARE PYRAMIDAL ARRANGEMENT. THE ORGANIC COFACTOR TOPA QUINONE (TPQ) IS IN THE ACTIVE SITE WITH THE NEAREST QUINONE OXYGEN ATOM AT ~6A FROM THE COPPER ATOM. |
| Chain | Residue |
| B | HIS603 |
| B | CU650 |
| B | HOH658 |
| B | HOH659 |
| B | TPQ387 |
| B | HIS442 |
| B | HIS444 |
Functional Information from PROSITE/UniProt
| site_id | PS01164 |
| Number of Residues | 14 |
| Details | COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LIVrtivTvgNYDN |
| Chain | Residue | Details |
| A | LEU376-ASN389 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ASP300 | |
| B | ASP300 | |
| 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 | TPQ387 | |
| B | TPQ387 | |
| Chain | Residue | Details |
| A | PHE298 | |
| B | PHE298 | |
| Chain | Residue | Details |
| A | VAL384 | |
| B | VAL384 | |
| Chain | Residue | Details |
| A | HIS442 | |
| B | HIS444 | |
| B | ASP451 | |
| B | PHE452 | |
| B | ASP453 | |
| B | ASP592 | |
| B | ILE593 | |
| B | HIS603 | |
| A | HIS444 | |
| A | ASP451 | |
| A | PHE452 | |
| A | ASP453 | |
| A | ASP592 | |
| A | ILE593 | |
| A | HIS603 | |
| B | HIS442 | |
| Chain | Residue | Details |
| A | TPQ387 | |
| B | TPQ387 | |
| Chain | Residue | Details |
| A | ASN131 | |
| B | ASN131 | |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305 |
| Chain | Residue | Details |
| A | ASN364 | |
| B | ASN364 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oac |
| Chain | Residue | Details |
| A | ASP300 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oac |
| Chain | Residue | Details |
| B | ASP300 | |
