1RDQ
Hydrolysis of ATP in the crystal of Y204A mutant of cAMP-dependent protein kinase
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | E | cAMP-dependent protein kinase, alpha-catalytic subunit | polymer | 350 | 40565.2 | 1 | UniProt (P05132) Pfam (PF00069) In PDB | Mus musculus (house mouse) | PKA C-alpha |
| 2 | I | cAMP-dependent protein kinase inhibitor, alpha form | polymer | 20 | 2226.4 | 1 | PKI-alpha, cAMP-dependent protein kinase inhibitor, muscle/brain isoform | ||
| 3 | E | PHOSPHATE ION | non-polymer | 95.0 | 1 | Chemie (PO4) | |||
| 4 | E | MAGNESIUM ION | non-polymer | 24.3 | 2 | Chemie (MG) | |||
| 5 | E | ADENOSINE-5'-DIPHOSPHATE | non-polymer | 427.2 | 1 | Chemie (ADP) | |||
| 6 | E | ADENOSINE-5'-TRIPHOSPHATE | non-polymer | 507.2 | 1 | Chemie (ATP) | |||
| 7 | E | (4R)-2-METHYLPENTANE-2,4-DIOL | non-polymer | 118.2 | 1 | Chemie (MRD) | |||
| 8 | E | GLYCEROL | non-polymer | 92.1 | 1 | Chemie (GOL) | |||
| 9 | water | water | 18.0 | 439 | Chemie (HOH) |
Sequence modifications
E: 1 - 350 (UniProt: P05132)
| PDB | External Database | Details |
|---|---|---|
| Tpo 197 | Thr 197 | modified residue |
| Ala 204 | Tyr 204 | engineered mutation |
| Sep 338 | Ser 338 | modified residue |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 42791.6 | |
| Non-Polymers* | Number of molecules | 7 |
| Total formula weight | 1288.2 | |
| All* | Total formula weight | 44079.9 |
