2BWD
Atomic Resolution Structure of Achromobacter cycloclastes Cu Nitrite Reductase with Endogenously bound Nitrite and NO
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 | 5 |
| Details | BINDING SITE FOR RESIDUE CU A 502 |
| Chain | Residue |
| A | HIS100 |
| A | HIS135 |
| A | HIS306 |
| A | HOA506 |
| A | NO2507 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 504 |
| Chain | Residue |
| A | THR228 |
| A | GLY229 |
| A | HIS319 |
| A | LYS321 |
| A | HOH2340 |
| A | HOH2556 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ACT A 505 |
| Chain | Residue |
| A | GLY225 |
| A | THR228 |
| A | PHE312 |
| A | HIS319 |
| A | HOH2144 |
| A | HOH2557 |
| A | HOH2558 |
| A | HOH2559 |
| A | HOH2560 |
| A | HOH2561 |
| A | HOH2562 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE NO2 A 507 |
| Chain | Residue |
| A | ASP98 |
| A | HIS100 |
| A | HIS135 |
| A | HIS255 |
| A | ILE257 |
| A | HIS306 |
| A | CU502 |
| A | HOA506 |
| A | HOH2235 |
| A | HOH2238 |
| A | HOH2563 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACT A 508 |
| Chain | Residue |
| A | TRP265 |
| A | THR267 |
| A | GLY268 |
| A | LYS269 |
| A | ASN272 |
| A | ASP275 |
| A | GLN278 |
| A | HOH2466 |
| A | HOH2564 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MLI A 503 |
| Chain | Residue |
| A | ARG250 |
| A | ASP251 |
| A | ARG253 |
| A | ASN307 |
| A | GLU310 |
| A | HOH2448 |
| A | HOH2554 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE HOA A 506 |
| Chain | Residue |
| A | ASP98 |
| A | HIS100 |
| A | HIS135 |
| A | ILE257 |
| A | HIS306 |
| A | CU502 |
| A | NO2507 |
| A | HOH2238 |
| A | HOH2563 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 164 |
| Details | Domain: {"description":"Plastocyanin-like 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"type 1 copper site"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"type 2 copper site"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| A | PHE64 | |
| A | GLY66 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| 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 |
