5I6M
Crystal Structure of Copper Nitrite Reductase at 100K after 7.59 MGy
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
| 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 | HOH876 |
| A | HIS100 |
| A | HIS135 |
| A | HIS306 |
| A | NO2505 |
| A | NO506 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 503 |
| Chain | Residue |
| A | THR228 |
| A | GLY229 |
| A | HIS319 |
| A | LYS321 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MLI A 504 |
| Chain | Residue |
| A | GLY225 |
| A | PHE312 |
| A | HIS319 |
| A | HOH750 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue NO2 A 505 |
| Chain | Residue |
| A | ASP98 |
| A | HIS100 |
| A | HIS135 |
| A | HIS255 |
| A | ILE257 |
| A | HIS306 |
| A | CU502 |
| A | NO506 |
| A | HOH824 |
| A | HOH841 |
| A | HOH876 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue NO A 506 |
| Chain | Residue |
| A | ASP98 |
| A | HIS100 |
| A | HIS135 |
| A | HIS255 |
| A | ILE257 |
| A | HIS306 |
| A | CU502 |
| A | NO2505 |
| A | HOH824 |
| A | HOH841 |
| A | HOH876 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue NO2 A 507 |
| Chain | Residue |
| A | ARG250 |
| A | ASP251 |
| A | ARG253 |
| A | ASN307 |
| A | NO2511 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue NO2 A 508 |
| Chain | Residue |
| A | ARG240 |
| A | HOH624 |
| A | HOH834 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue NO2 A 509 |
| Chain | Residue |
| A | TRP265 |
| A | ALA266 |
| A | THR267 |
| A | GLY268 |
| A | LYS269 |
| A | ASN272 |
| A | GLN278 |
| A | HOH696 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue NO2 A 510 |
| Chain | Residue |
| A | LYS125 |
| A | THR127 |
| A | ARG296 |
| A | LEU330 |
| A | HOH665 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue NO2 A 511 |
| Chain | Residue |
| A | ARG250 |
| A | ARG253 |
| A | ASN307 |
| A | GLU310 |
| A | NO2507 |
| A | HOH908 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue NO2 A 512 |
| Chain | Residue |
| A | GLY225 |
| A | ALA226 |
| A | THR228 |
| A | HIS231 |
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 | 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 |
| A | THR280 | electrostatic stabiliser, modifies pKa |
| A | HIS306 | metal ligand |
