5ZP3
Copper amine oxidase from Arthrobacter globiformis anaerobically reduced by ethylamine at pH 10 at 288 K (1)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005507 | molecular_function | copper ion binding |
A | 0008131 | molecular_function | primary amine oxidase activity |
A | 0009308 | biological_process | amine metabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
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 amine oxidase activity |
B | 0009308 | biological_process | amine metabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
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 | 6 |
Details | binding site for residue CU A 701 |
Chain | Residue |
A | TYQ382 |
A | HIS431 |
A | HIS433 |
A | HIS592 |
A | HOH960 |
A | HOH1166 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue NA A 702 |
Chain | Residue |
A | ILE582 |
A | HOH1023 |
A | ASP440 |
A | MET441 |
A | ASP581 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue NA A 703 |
Chain | Residue |
A | ALA93 |
A | ALA94 |
A | ARG148 |
A | SER562 |
A | HOH1175 |
B | GLU22 |
B | VAL79 |
B | THR80 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue EDO A 704 |
Chain | Residue |
A | LEU42 |
A | GLY43 |
A | VAL44 |
A | PHE249 |
A | ASP250 |
A | VAL251 |
A | VAL327 |
A | ILE328 |
A | HOH976 |
A | HOH1113 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue CU B 701 |
Chain | Residue |
B | TYQ382 |
B | HIS431 |
B | HIS433 |
B | HIS592 |
B | HOH1011 |
B | HOH1205 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue NA B 702 |
Chain | Residue |
B | ASP440 |
B | MET441 |
B | ASP581 |
B | ILE582 |
B | HOH1051 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue EDO B 703 |
Chain | Residue |
B | LEU42 |
B | GLY43 |
B | PHE249 |
B | ASP250 |
B | VAL251 |
B | VAL327 |
B | HOH926 |
B | HOH1084 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue EDO B 704 |
Chain | Residue |
B | ILE39 |
B | ALA40 |
B | TYR41 |
B | GLN306 |
B | SER329 |
B | HOH833 |
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 | TYQ382 | |
B | TYQ382 |
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 | TYQ382 | |
B | TYQ382 |