1NID
THE STRUCTURE OF CU-NITRITE REDUCTASE FROM ACHROMOBACTER CYCLOCLASTES AT FIVE PH VALUES, WITH NITRITE BOUND AND WITH TYPE II CU DEPLETED
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 | HIS145 |
A | MET150 |
A | HIS95 |
A | CYS136 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU A 502 |
Chain | Residue |
A | ASP98 |
A | HIS100 |
A | HIS135 |
A | HIS306 |
A | NO2503 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE NO2 A 503 |
Chain | Residue |
A | ASP98 |
A | HIS100 |
A | HIS135 |
A | HIS255 |
A | ILE257 |
A | HIS306 |
A | LEU308 |
A | CU502 |
site_id | CU1 |
Number of Residues | 4 |
Details | TYPE I SITE |
Chain | Residue |
A | HIS95 |
A | CYS136 |
A | HIS145 |
A | MET150 |
site_id | CU2 |
Number of Residues | 3 |
Details | TYPE II SITE |
Chain | Residue |
A | HIS100 |
A | HIS135 |
A | NO2503 |
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 | CSA1 |
Number of Residues | 2 |
Details | a catalytic site defined by CSA, PubMed 10811642, 9353305, 7499203, 8172899, 15475344, 11041837, 15182351 |
Chain | Residue | Details |
A | ASP98 | |
A | HIS255 |
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 |