1QL6
THE CATALYTIC MECHANISM OF PHOSPHORYLASE KINASE PROBED BY MUTATIONAL STUDIES
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | PHOSPHORYLASE KINASE | polymer | 298 | 34274.3 | 1 | UniProt (P00518) Pfam (PF00069) | ORYCTOLAGUS CUNICULUS (RABBIT) | RABBIT MUSCLE PHOSPHORYLASE KINASE |
| 2 | B (A) | ADENOSINE-5'-TRIPHOSPHATE | non-polymer | 507.2 | 1 | Chemie (ATP) | |||
| 3 | C, D (A) | MANGANESE (II) ION | non-polymer | 54.9 | 2 | Chemie (MN) | |||
| 4 | E (A) | SULFATE ION | non-polymer | 96.1 | 1 | Chemie (SO4) | |||
| 5 | F (A) | water | water | 18.0 | 104 | Chemie (HOH) |
Sequence modifications
A: 1 - 298 (UniProt: P00518)
| PDB | External Database | Details |
|---|---|---|
| Ser 182 | Glu 182 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 34274.3 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 713.1 | |
| All* | Total formula weight | 34987.4 |
