5I6N
Crystal Structure of Copper Nitrite Reductase at 100K after 11.73 MGy
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 | 4 |
Details | binding site for residue CU A 502 |
Chain | Residue |
A | HIS100 |
A | HIS135 |
A | HIS306 |
A | NO503 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue NO A 503 |
Chain | Residue |
A | HIS100 |
A | HIS135 |
A | HIS255 |
A | ILE257 |
A | HIS306 |
A | CU502 |
A | ASP98 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue NO2 A 504 |
Chain | Residue |
A | LYS33 |
A | LYS187 |
A | ASP188 |
A | GLU189 |
A | LYS194 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue NO2 A 505 |
Chain | Residue |
A | ARG250 |
A | ASP251 |
A | ARG253 |
A | NO2509 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue NO2 A 506 |
Chain | Residue |
A | ARG240 |
A | HOH628 |
A | HOH809 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue NO2 A 507 |
Chain | Residue |
A | TRP265 |
A | ALA266 |
A | THR267 |
A | GLY268 |
A | LYS269 |
A | ASN272 |
A | GLN278 |
A | HOH745 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue NO2 A 508 |
Chain | Residue |
A | LYS125 |
A | THR127 |
A | ARG296 |
A | HOH668 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue NO2 A 509 |
Chain | Residue |
A | ARG250 |
A | ARG253 |
A | ASN307 |
A | GLU310 |
A | NO2505 |
A | HOH601 |
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 |