4G38
Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A | Sulfite reductase [NADPH] hemoprotein beta-component | polymer | 570 | 64163.2 | 1 | UniProt (P17846) Pfam (PF03460) Pfam (PF01077) In PDB | Escherichia coli | SiR-HP, SiRHP |
| 2 | A | PHOSPHATE ION | non-polymer | 95.0 | 1 | Chemie (PO4) | |||
| 3 | A | POTASSIUM ION | non-polymer | 39.1 | 1 | Chemie (K) | |||
| 4 | A | IRON/SULFUR CLUSTER | non-polymer | 351.6 | 1 | Chemie (SF4) | |||
| 5 | A | SIROHEME | non-polymer | 916.7 | 1 | Chemie (SRM) | |||
| 6 | water | water | 18.0 | 564 | Chemie (HOH) |
Sequence modifications
A: 74 - 570 (UniProt: P17846)
| PDB | External Database | Details |
|---|---|---|
| Trp 149 | Asn 149 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 64163.2 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 1402.4 | |
| All* | Total formula weight | 65565.6 |
