2C4M
Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control.
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, D | GLYCOGEN PHOSPHORYLASE | polymer | 796 | 90662.9 | 4 | UniProt (Q8KQ56) Pfam (PF00343) In PDB | CORYNEBACTERIUM CALLUNAE | STARCH PHOSPHORYLASE |
2 | A, D, B, C | PYRIDOXAL-5'-PHOSPHATE | non-polymer | 247.1 | 4 | Chemie (PLP) | |||
3 | C, A, D, B | PHOSPHATE ION | non-polymer | 95.0 | 9 | Chemie (PO4) | |||
4 | C, A, D, B | FORMIC ACID | non-polymer | 46.0 | 19 | Chemie (FMT) | |||
5 | C, B | 1,2-ETHANEDIOL | non-polymer | 62.1 | 3 | Chemie (EDO) | |||
6 | water | water | 18.0 | 1154 | Chemie (HOH) |
Sequence modifications
A, B, C, D: 0 - 795 (UniProt: Q8KQ56)
PDB | External Database | Details |
---|---|---|
Ala 224 | Ser 225 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 4 |
Total formula weight | 362651.7 | |
Non-Polymers* | Number of molecules | 35 |
Total formula weight | 2904.0 | |
All* | Total formula weight | 365555.7 |