2IUO
Site Directed Mutagenesis of Key Residues Involved in the Catalytic Mechanism of Cyanase
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, E... (A, B, C, D, E...) | CYANATE HYDRATASE | polymer | 156 | 17037.8 | 10 | UniProt (P00816) Pfam (PF21291) Pfam (PF02560) | ESCHERICHIA COLI | CYANASE LYASE, CYANASE, CYANATE HYDROLASE |
| 2 | CA, HA, K, LA, O... (E, F, A, G, B...) | BROMIDE ION | non-polymer | 79.9 | 10 | Chemie (BR) | |||
| 3 | DA, IA, L, MA, P... (E, F, A, G, B...) | CHLORIDE ION | non-polymer | 35.5 | 10 | Chemie (CL) | |||
| 4 | AA, AB, BA, BB, EA... (D, J, E, F, A...) | SULFATE ION | non-polymer | 96.1 | 23 | Chemie (SO4) | |||
| 5 | S (B) | AZIDE ION | non-polymer | 42.0 | 1 | Chemie (AZI) | |||
| 6 | CB, DB, EB, FB, GB... (A, B, C, D, E...) | water | water | 18.0 | 2052 | Chemie (HOH) |
Sequence modifications
A, B, C, D, E, F, G, H, I, J: 1 - 156 (UniProt: P00816)
| PDB | External Database | Details |
|---|---|---|
| Gly 122 | Ser 122 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 10 |
| Total formula weight | 170377.7 | |
| Non-Polymers* | Number of molecules | 44 |
| Total formula weight | 3405.0 | |
| All* | Total formula weight | 173782.7 |
