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 (A, B) | Catabolite gene activator | polymer | 210 | 23732.5 | 2 | UniProt (P0ACJ8) Pfam (PF00027) Pfam (PF13545) | Escherichia coli | cAMP receptor protein, cAMP regulatory protein |
| 2 | C, D, F, G (A, B) | ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE | non-polymer | 329.2 | 4 | Chemie (CMP) PubChem (6076) PubChem (216878) PubChem (3080770) PubChem (3246347) PubChem (6603718) PubChem (6713792) PubChem (6714006) PubChem (12071879) PubChem (12866365) PubChem (23902375) PubChem (25322948) PubChem (40467852) PubChem (44629928) PubChem (176488666) PubChem (25322946) PubChem (59350541) PubChem (274) PubChem (6604194) PubChem (56973690) PubChem (163043517) PubChem (59909322) PubChem (59968988) PubChem (70878457) PubChem (124132380) PubChem (129317551) PubChem (131841987) PubChem (134693155) PubChem (138107790) PubChem (163043518) | |||
| 3 | E (A) | PHOSPHATE ION | non-polymer | 95.0 | 1 | Chemie (PO4) PubChem (1061) | |||
| 4 | H, I (A, B) | 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 |
