1KSI
CRYSTAL STRUCTURE OF A EUKARYOTIC (PEA SEEDLING) COPPER-CONTAINING AMINE OXIDASE AT 2.2A RESOLUTION
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 | 0016641 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor |
| A | 0048038 | molecular_function | quinone binding |
| 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 | 0016641 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor |
| B | 0048038 | molecular_function | quinone binding |
| 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 | CU702 |
| A | HOH1051 |
| A | HOH978 |
| 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 | CU702 |
| B | HOH1087 |
| B | HOH951 |
| 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
| site_id | SWS_FT_FI1 |
| Number of Residues | 50 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P12807","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Schiff-base intermediate with substrate; via topaquinone","evidences":[{"source":"UniProtKB","id":"P12807","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P12807","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8805580","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KSI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"2',4',5'-topaquinone","evidences":[{"source":"PubMed","id":"8805580","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KSI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"8805580","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KSI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
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 |
