6KNF
CryoEM map and model of Nitrite Reductase at pH 6.2
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 |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019333 | biological_process | denitrification pathway |
| B | 0042128 | biological_process | nitrate assimilation |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
| C | 0005507 | molecular_function | copper ion binding |
| C | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019333 | biological_process | denitrification pathway |
| C | 0042128 | biological_process | nitrate assimilation |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0046872 | molecular_function | metal ion binding |
| C | 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 500 |
| Chain | Residue |
| A | HIS95 |
| A | CYS136 |
| A | HIS145 |
| A | MET150 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CU A 501 |
| Chain | Residue |
| A | HIS100 |
| A | HIS135 |
| C | HIS306 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CU B 500 |
| Chain | Residue |
| B | HIS145 |
| B | MET150 |
| B | HIS95 |
| B | CYS136 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue CU B 501 |
| Chain | Residue |
| A | HIS306 |
| B | HIS100 |
| B | HIS135 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CU C 500 |
| Chain | Residue |
| C | HIS95 |
| C | CYS136 |
| C | HIS145 |
| C | MET150 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue CU C 501 |
| Chain | Residue |
| B | HIS306 |
| C | HIS100 |
| C | HIS135 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: type 1 copper site |
| Chain | Residue | Details |
| A | HIS95 | |
| C | CYS136 | |
| C | HIS145 | |
| C | MET150 | |
| A | CYS136 | |
| A | HIS145 | |
| A | MET150 | |
| B | HIS95 | |
| B | CYS136 | |
| B | HIS145 | |
| B | MET150 | |
| C | HIS95 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | BINDING: type 2 copper site |
| Chain | Residue | Details |
| A | HIS100 | |
| A | HIS135 | |
| A | HIS306 | |
| B | HIS100 | |
| B | HIS135 | |
| B | HIS306 | |
| C | HIS100 | |
| C | HIS135 | |
| C | 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 |
| site_id | MCSA2 |
| Number of Residues | 11 |
| Details | M-CSA 4 |
| Chain | Residue | Details |
| B | HIS95 | metal ligand |
| B | THR280 | electrostatic stabiliser, modifies pKa |
| B | HIS306 | metal ligand |
| B | ASP98 | activator, hydrogen bond acceptor, proton acceptor, proton donor |
| B | HIS100 | metal ligand |
| B | HIS135 | metal ligand, single electron acceptor, single electron donor, single electron relay |
| B | CYS136 | metal ligand, single electron acceptor, single electron donor, single electron relay |
| B | HIS145 | metal ligand |
| B | MET150 | metal ligand |
| B | HIS255 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU279 | electrostatic stabiliser, modifies pKa |
| site_id | MCSA3 |
| Number of Residues | 11 |
| Details | M-CSA 4 |
| Chain | Residue | Details |
| C | HIS95 | metal ligand |
| C | THR280 | electrostatic stabiliser, modifies pKa |
| C | HIS306 | metal ligand |
| C | ASP98 | activator, hydrogen bond acceptor, proton acceptor, proton donor |
| C | HIS100 | metal ligand |
| C | HIS135 | metal ligand, single electron acceptor, single electron donor, single electron relay |
| C | CYS136 | metal ligand, single electron acceptor, single electron donor, single electron relay |
| C | HIS145 | metal ligand |
| C | MET150 | metal ligand |
| C | HIS255 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | GLU279 | electrostatic stabiliser, modifies pKa |
