2Y73
THE NATIVE STRUCTURES OF SOLUBLE HUMAN PRIMARY AMINE OXIDASE AOC3
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005507 | molecular_function | copper ion binding |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005769 | cellular_component | early endosome |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005794 | cellular_component | Golgi apparatus |
A | 0005886 | cellular_component | plasma membrane |
A | 0005902 | cellular_component | microvillus |
A | 0006954 | biological_process | inflammatory response |
A | 0007155 | biological_process | cell adhesion |
A | 0008131 | molecular_function | primary methylamine oxidase activity |
A | 0009308 | biological_process | amine metabolic process |
A | 0009986 | cellular_component | cell surface |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016641 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0046982 | molecular_function | protein heterodimerization activity |
A | 0048038 | molecular_function | quinone binding |
A | 0052595 | molecular_function | aliphatic amine oxidase activity |
B | 0005507 | molecular_function | copper ion binding |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005769 | cellular_component | early endosome |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0005794 | cellular_component | Golgi apparatus |
B | 0005886 | cellular_component | plasma membrane |
B | 0005902 | cellular_component | microvillus |
B | 0006954 | biological_process | inflammatory response |
B | 0007155 | biological_process | cell adhesion |
B | 0008131 | molecular_function | primary methylamine oxidase activity |
B | 0009308 | biological_process | amine metabolic process |
B | 0009986 | cellular_component | cell surface |
B | 0016020 | cellular_component | membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016641 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0046982 | molecular_function | protein heterodimerization activity |
B | 0048038 | molecular_function | quinone binding |
B | 0052595 | molecular_function | aliphatic amine oxidase activity |
Functional Information from PROSITE/UniProt
site_id | PS01164 |
Number of Residues | 14 |
Details | COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVVrsmsTllNYDY |
Chain | Residue | Details |
A | LEU460-TYR473 |
site_id | PS01165 |
Number of Residues | 14 |
Details | COPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TaGflHIphaEDiP |
Chain | Residue | Details |
A | THR679-PRO692 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:9653080 |
Chain | Residue | Details |
A | MET1-THR5 | |
B | MET1-THR5 |
site_id | SWS_FT_FI2 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Signal-anchor for type II membrane protein => ECO:0000255 |
Chain | Residue | Details |
A | ILE6-VAL26 | |
B | ILE6-VAL26 |
site_id | SWS_FT_FI3 |
Number of Residues | 1472 |
Details | TOPO_DOM: Extracellular => ECO:0000305|PubMed:9653080 |
Chain | Residue | Details |
A | GLY27-ASN763 | |
B | GLY27-ASN763 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P19801 |
Chain | Residue | Details |
A | ASP386 | |
B | ASP386 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | ACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0000269|PubMed:16046623, ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1 |
Chain | Residue | Details |
A | TPQ471 | |
B | TPQ471 |
site_id | SWS_FT_FI6 |
Number of Residues | 26 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1, ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY |
Chain | Residue | Details |
A | HIS520 | |
A | GLU667 | |
A | ASP673 | |
A | LEU674 | |
A | HIS684 | |
B | HIS520 | |
B | HIS522 | |
B | ASP529 | |
B | LEU530 | |
B | ASP531 | |
B | GLU572 | |
A | HIS522 | |
B | GLU641 | |
B | PHE663 | |
B | ASN665 | |
B | GLU667 | |
B | ASP673 | |
B | LEU674 | |
B | HIS684 | |
A | ASP529 | |
A | LEU530 | |
A | ASP531 | |
A | GLU572 | |
A | GLU641 | |
A | PHE663 | |
A | ASN665 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:16046623, ECO:0007744|PDB:1PU4 |
Chain | Residue | Details |
A | TPQ471 | |
B | TPQ471 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | CARBOHYD: O-linked (GalNAc...) serine => ECO:0000305|PubMed:16046623 |
Chain | Residue | Details |
A | SER43 | |
B | SER43 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:19159218, ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1 |
Chain | Residue | Details |
A | ASN137 | |
B | ASN137 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | CARBOHYD: O-linked (GalNAc...) threonine => ECO:0000305|PubMed:16046623 |
Chain | Residue | Details |
A | THR212 | |
B | THR212 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1, ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY |
Chain | Residue | Details |
A | ASN232 | |
B | ASN232 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:4BTY |
Chain | Residue | Details |
A | ASN294 | |
B | ASN294 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY |
Chain | Residue | Details |
A | ASN592 | |
B | ASN592 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX |
Chain | Residue | Details |
A | ASN618 | |
B | ASN618 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY |
Chain | Residue | Details |
A | ASN666 | |
B | ASN666 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | CARBOHYD: O-linked (GlcNAc) threonine => ECO:0000305|PubMed:16046623 |
Chain | Residue | Details |
A | THR679 | |
B | THR679 |