5N8F
Serial Cu nitrite reductase structures at elevated cryogenic temperature, 240K. Dataset 1.
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 501 |
| Chain | Residue |
| A | HIS95 |
| A | CYS136 |
| A | HIS145 |
| A | MET150 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CU A 502 |
| Chain | Residue |
| A | HOH820 |
| A | HIS100 |
| A | HIS135 |
| A | ILE257 |
| A | HIS306 |
| A | HOH801 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 503 |
| Chain | Residue |
| A | THR228 |
| A | GLY229 |
| A | HIS319 |
| A | LYS321 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | LYS125 |
| A | ARG296 |
| A | SO4508 |
| A | HOH720 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 505 |
| Chain | Residue |
| A | PRO158 |
| A | ARG159 |
| A | ASP160 |
| A | HOH606 |
| A | HOH631 |
| A | HOH669 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 A 506 |
| Chain | Residue |
| A | ARG123 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 507 |
| Chain | Residue |
| A | LYS33 |
| A | ASP188 |
| A | GLU189 |
| A | LYS194 |
| A | HOH736 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 508 |
| Chain | Residue |
| A | THR127 |
| A | LYS128 |
| A | ARG271 |
| A | ARG296 |
| A | SO4504 |
| A | HOH667 |
| A | HOH757 |
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 |
