Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005507 | molecular_function | copper ion binding |
A | 0006518 | biological_process | peptide metabolic process |
A | 0016020 | cellular_component | membrane |
A | 0016715 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CU A 401 |
Chain | Residue |
A | HIS107 |
A | HIS108 |
A | HIS172 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU A 402 |
Chain | Residue |
A | HIS242 |
A | HIS244 |
A | MET314 |
A | PEO404 |
A | HOH539 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NI A 403 |
Chain | Residue |
A | HIS305 |
A | HOH547 |
A | HIS235 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PEO A 404 |
Chain | Residue |
A | GLU128 |
A | HIS242 |
A | HIS244 |
A | MET314 |
A | CU402 |
A | HOH539 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 405 |
Chain | Residue |
A | LEU138 |
A | TYR139 |
A | THR148 |
A | MET320 |
A | HOH546 |
A | HOH559 |
A | HOH567 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 406 |
Chain | Residue |
A | TYR205 |
A | GLN228 |
A | TYR229 |
A | LYS230 |
A | MET231 |
A | THR333 |
A | HOH644 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 407 |
Chain | Residue |
A | VAL255 |
A | ARG256 |
A | ASN257 |
A | GLY258 |
A | GLY286 |
A | ILE288 |
A | HOH621 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 408 |
Chain | Residue |
A | GLY113 |
A | ASN136 |
A | LEU138 |
A | ARG157 |
A | GLY163 |
A | SER164 |
A | HOH589 |
A | HOH590 |
Functional Information from PROSITE/UniProt
site_id | PS00084 |
Number of Residues | 8 |
Details | CU2_MONOOXYGENASE_1 Copper type II, ascorbate-dependent monooxygenases signature 1. HHMllFgC |
Chain | Residue | Details |
A | HIS107-CYS114 | |
site_id | PS00085 |
Number of Residues | 13 |
Details | CU2_MONOOXYGENASE_2 Copper type II, ascorbate-dependent monooxygenases signature 2. HvFayrvHTHhlG |
Chain | Residue | Details |
A | HIS235-GLY247 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS107 | |
A | HIS108 | |
A | HIS172 | |
A | HIS242 | |
A | HIS244 | |
A | MET314 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 135 |
Chain | Residue | Details |
A | HIS107 | metal ligand |
A | HIS108 | hydrogen bond donor, metal ligand, single electron acceptor, single electron donor, single electron relay |
A | GLN170 | hydrogen bond acceptor, single electron acceptor, single electron donor, single electron relay |
A | HIS172 | metal ligand |
A | HIS242 | metal ligand |
A | HIS244 | metal ligand |
A | MET314 | metal ligand |