5OF8
Cu nitrite reductase serial data at varying temperatures 190K 0.48MGy
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019333 | biological_process | denitrification pathway |
| A | 0042128 | biological_process | nitrate assimilation |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue CU A 401 |
| Chain | Residue |
| A | HIS95 |
| A | CYS136 |
| A | HIS145 |
| A | MET150 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CU A 402 |
| Chain | Residue |
| A | HIS100 |
| A | HIS135 |
| A | HIS306 |
| A | NO410 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue NO2 A 403 |
| Chain | Residue |
| A | PRO69 |
| A | ASN151 |
| A | GLY179 |
| A | GLU180 |
| A | GLN181 |
| A | HOH533 |
| A | VAL68 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue NO2 A 404 |
| Chain | Residue |
| A | VAL335 |
| A | LYS336 |
| A | HOH546 |
| A | HOH588 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue ACT A 405 |
| Chain | Residue |
| A | TRP265 |
| A | THR267 |
| A | GLY268 |
| A | LYS269 |
| A | ASN272 |
| A | GLN278 |
| A | HOH503 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 A 406 |
| Chain | Residue |
| A | ARG123 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 407 |
| Chain | Residue |
| A | LYS33 |
| A | ASP188 |
| A | GLU189 |
| A | LYS194 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue NO2 A 408 |
| Chain | Residue |
| A | ARG211 |
| A | THR216 |
| A | HIS217 |
| A | VAL224 |
| A | LEU314 |
| A | HOH701 |
| A | HOH708 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue NO A 409 |
| Chain | Residue |
| A | PRO88 |
| A | ASP89 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue NO A 410 |
| Chain | Residue |
| A | ASP98 |
| A | HIS100 |
| A | HIS135 |
| A | ILE257 |
| A | HIS306 |
| A | CU402 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: type 1 copper site |
| Chain | Residue | Details |
| A | HIS95 | |
| A | CYS136 | |
| A | HIS145 | |
| A | MET150 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: type 2 copper site |
| Chain | Residue | Details |
| A | HIS100 | |
| A | HIS135 | |
| A | HIS306 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 11 |
| Details | M-CSA 4 |
| Chain | Residue | Details |
| A | HIS95 | metal ligand |
| A | THR280 | electrostatic stabiliser, modifies pKa |
| A | HIS306 | metal ligand |
| A | ASP98 | activator, hydrogen bond acceptor, proton acceptor, proton donor |
| A | HIS100 | metal ligand |
| A | HIS135 | metal ligand, single electron acceptor, single electron donor, single electron relay |
| A | CYS136 | metal ligand, single electron acceptor, single electron donor, single electron relay |
| A | HIS145 | metal ligand |
| A | MET150 | metal ligand |
| A | HIS255 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU279 | electrostatic stabiliser, modifies pKa |
