5OF6
Cu nitrite reductase serial data at varying temperatures 190K 0.48MGy
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 401 |
| Chain | Residue |
| A | HIS95 |
| A | CYS136 |
| A | HIS145 |
| A | MET150 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CU A 402 |
| Chain | Residue |
| A | HIS100 |
| A | HIS135 |
| A | HIS306 |
| A | NO2407 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | ARG159 |
| A | ASP160 |
| A | HOH523 |
| A | HOH524 |
| A | HOH600 |
| A | HOH630 |
| A | HOH862 |
| A | PRO158 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue NO2 A 404 |
| Chain | Residue |
| A | VAL68 |
| A | PRO69 |
| A | ASN151 |
| A | GLY179 |
| A | GLU180 |
| A | GLN181 |
| A | HOH509 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue NO2 A 405 |
| Chain | Residue |
| A | LEU93 |
| A | LEU94 |
| A | MET141 |
| A | GLY324 |
| A | GLU325 |
| A | HOH606 |
| A | HOH723 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue NO2 A 406 |
| Chain | Residue |
| A | VAL335 |
| A | LYS336 |
| A | HOH538 |
| A | HOH566 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue NO2 A 407 |
| Chain | Residue |
| A | ASP98 |
| A | HIS100 |
| A | HIS135 |
| A | HIS255 |
| A | ILE257 |
| A | HIS306 |
| A | CU402 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue NO2 A 408 |
| Chain | Residue |
| A | GLN113 |
| A | ASN115 |
| A | GLU118 |
| A | PRO337 |
| A | HOH534 |
| A | HOH686 |
| A | HOH859 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue ACT A 409 |
| Chain | Residue |
| A | TRP265 |
| A | THR267 |
| A | GLY268 |
| A | LYS269 |
| A | ASN272 |
| A | ASP275 |
| A | GLN278 |
| A | HOH515 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue ACT A 410 |
| Chain | Residue |
| A | PHE24 |
| A | LYS174 |
| A | TYR176 |
| A | THR234 |
| A | HOH525 |
| A | HOH527 |
| A | HOH667 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 411 |
| Chain | Residue |
| A | ALA27 |
| A | ARG37 |
| A | HOH507 |
| A | HOH510 |
| A | HOH531 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 412 |
| Chain | Residue |
| A | THR228 |
| A | GLY229 |
| A | HIS319 |
| A | LYS321 |
| A | HOH804 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 413 |
| Chain | Residue |
| A | ARG123 |
| A | HOH557 |
| A | HOH567 |
| A | HOH714 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 414 |
| Chain | Residue |
| A | LYS125 |
| A | THR127 |
| A | ARG296 |
| A | LEU330 |
| A | HOH545 |
| A | HOH672 |
| site_id | AD6 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 415 |
| Chain | Residue |
| A | ASP29 |
| A | LYS33 |
| A | ASP188 |
| A | GLU189 |
| A | LYS194 |
| A | HOH866 |
| A | HOH907 |
| site_id | AD7 |
| Number of Residues | 10 |
| Details | binding site for residue MLI A 416 |
| Chain | Residue |
| A | HOH680 |
| A | GLY225 |
| A | PHE312 |
| A | HIS319 |
| A | HOH504 |
| A | HOH565 |
| A | HOH601 |
| A | HOH618 |
| A | HOH646 |
| A | HOH659 |
| site_id | AD8 |
| Number of Residues | 9 |
| Details | binding site for residue NO2 A 417 |
| Chain | Residue |
| A | TYR193 |
| A | ARG211 |
| A | THR216 |
| A | HIS217 |
| A | VAL224 |
| A | LEU314 |
| A | HOH520 |
| A | HOH773 |
| A | HOH790 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue NO A 418 |
| Chain | Residue |
| A | PRO88 |
| A | ASP89 |
| A | HOH772 |
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 |
