3RPQ
Domain-domain flexibility leads to allostery within the camp receptor protein (CRP)
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B | Catabolite gene activator | polymer | 210 | 23732.5 | 2 | UniProt (P0ACJ8) Pfam (PF00027) Pfam (PF13545) In PDB | Escherichia coli | cAMP receptor protein, cAMP regulatory protein |
| 2 | A, B | ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE | non-polymer | 329.2 | 4 | Chemie (CMP) | |||
| 3 | A | PHOSPHATE ION | non-polymer | 95.0 | 1 | Chemie (PO4) | |||
| 4 | water | water | 18.0 | 15 | Chemie (HOH) |
Sequence modifications
A, B: 0 - 209 (UniProt: P0ACJ8)
| PDB | External Database | Details |
|---|---|---|
| Phe 62 | Ser 63 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 47465.1 | |
| Non-Polymers* | Number of molecules | 5 |
| Total formula weight | 1411.8 | |
| All* | Total formula weight | 48876.9 |
