3O20
Electron transfer complexes:experimental mapping of the Redox-dependent Cytochrome C electrostatic surface
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B, C | Cytochrome c | polymer | 105 | 11751.6 | 3 | UniProt (P00004) Pfam (PF00034) In PDB | Equus caballus (domestic horse equine) | |
| 2 | A, B, C | HEME C | non-polymer | 618.5 | 3 | Chemie (HEC) | |||
| 3 | A, B, C | NITRATE ION | non-polymer | 62.0 | 18 | Chemie (NO3) | |||
| 4 | water | water | 18.0 | 365 | Chemie (HOH) |
Sequence modifications
A, B, C: 1 - 104 (UniProt: P00004)
| PDB | External Database | Details |
|---|---|---|
| Ace 0 | - | acetylation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 3 |
| Total formula weight | 35254.9 | |
| Non-Polymers* | Number of molecules | 21 |
| Total formula weight | 2971.6 | |
| All* | Total formula weight | 38226.5 |
