1EKM
CRYSTAL STRUCTURE AT 2.5 A RESOLUTION OF ZINC-SUBSTITUTED COPPER AMINE OXIDASE OF HANSENULA POLYMORPHA EXPRESSED IN ESCHERICHIA COLI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005777 | cellular_component | peroxisome |
| 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 | 0005777 | cellular_component | peroxisome |
| 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 |
| C | 0005507 | molecular_function | copper ion binding |
| C | 0005777 | cellular_component | peroxisome |
| C | 0008131 | molecular_function | primary methylamine oxidase activity |
| C | 0009308 | biological_process | amine metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016641 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0048038 | molecular_function | quinone binding |
| C | 0052595 | molecular_function | aliphatic amine oxidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 701 |
| Chain | Residue |
| A | TYR405 |
| A | HIS456 |
| A | HIS458 |
| A | HIS624 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 701 |
| Chain | Residue |
| B | TYR405 |
| B | HIS456 |
| B | HIS458 |
| B | HIS624 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 701 |
| Chain | Residue |
| C | HIS456 |
| C | HIS458 |
| C | HIS624 |
| C | TYR405 |
Functional Information from PROSITE/UniProt
| site_id | PS01159 |
| Number of Residues | 26 |
| Details | WW_DOMAIN_1 WW/rsp5/WWP domain signature. WgtgkrlqqalvYYrsdedd.SQYSHP |
| Chain | Residue | Details |
| A | TRP164-PRO189 |
| site_id | PS01164 |
| Number of Residues | 14 |
| Details | COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVVsqifTaaNYEY |
| Chain | Residue | Details |
| A | LEU394-TYR407 |
| site_id | PS01165 |
| Number of Residues | 14 |
| Details | COPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TfGitHFpapEDfP |
| Chain | Residue | Details |
| A | THR619-PRO632 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:9551552 |
| Chain | Residue | Details |
| A | ASP319 | |
| B | ASP319 | |
| C | ASP319 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | ACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4KFF |
| Chain | Residue | Details |
| A | TYR405 | |
| B | TYR405 | |
| C | TYR405 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5 |
| Chain | Residue | Details |
| A | ALA317 | |
| B | ALA317 | |
| C | ALA317 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P46883 |
| Chain | Residue | Details |
| A | ALA402 | |
| B | ALA402 | |
| C | ALA402 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV, ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD, ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF |
| Chain | Residue | Details |
| A | HIS456 | |
| A | HIS458 | |
| A | HIS624 | |
| B | HIS456 | |
| B | HIS458 | |
| B | HIS624 | |
| C | HIS456 | |
| C | HIS458 | |
| C | HIS624 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q43077 |
| Chain | Residue | Details |
| A | ASP465 | |
| A | ASP613 | |
| A | ILE614 | |
| B | ASP465 | |
| B | ASP613 | |
| B | ILE614 | |
| C | ASP465 | |
| C | ASP613 | |
| C | ILE614 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | MOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:2OQE |
| Chain | Residue | Details |
| A | TYR405 | |
| B | TYR405 | |
| C | TYR405 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:9551552 |
| Chain | Residue | Details |
| A | ASN243 | |
| B | ASN243 | |
| C | ASN243 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oac |
| Chain | Residue | Details |
| A | ASP319 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oac |
| Chain | Residue | Details |
| B | ASP319 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oac |
| Chain | Residue | Details |
| C | ASP319 |
