3ZBM
Structure of M92A variant of three-domain heme-Cu nitrite reductase from Ralstonia pickettii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0020037 | molecular_function | heme binding |
| 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 1460 |
| Chain | Residue |
| A | HIS94 |
| A | CYS135 |
| A | HIS143 |
| A | MET148 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CU A 1461 |
| Chain | Residue |
| A | HOH2310 |
| A | HIS99 |
| A | HIS134 |
| A | HIS240 |
| A | HIS289 |
| A | HOH2136 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEM A 1462 |
| Chain | Residue |
| A | THR363 |
| A | CYS364 |
| A | VAL366 |
| A | CYS367 |
| A | HIS368 |
| A | PRO380 |
| A | PRO381 |
| A | LEU382 |
| A | SER385 |
| A | PHE387 |
| A | ASN404 |
| A | GLY405 |
| A | SER416 |
| A | VAL417 |
| A | MET418 |
| A | MET421 |
