4HZP
The Structure of the Bifunctional Acetyltransferase/Decarboxylase LnmK from the Leinamycin Biosynthetic Pathway Revealing Novel Activity for a Double Hot Dog Fold
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A | Bifunctional methylmalonyl-CoA:ACP Acyltransferase/Decarboxylase | polymer | 318 | 35263.3 | 1 | UniProt (Q8GGP1) Pfam (PF18238) In PDB | Streptomyces atroolivaceus | |
| 2 | A | COENZYME A | non-polymer | 767.5 | 1 | Chemie (COA) | |||
| 3 | A | CHLORIDE ION | non-polymer | 35.5 | 1 | Chemie (CL) | |||
| 4 | A | SULFATE ION | non-polymer | 96.1 | 2 | Chemie (SO4) | |||
| 5 | water | water | 18.0 | 160 | Chemie (HOH) |
Sequence modifications
A: 2 - 319 (UniProt: Q8GGP1)
| PDB | External Database | Details |
|---|---|---|
| Ser 2 | Thr 2 | engineered mutation |
| Phe 62 | Tyr 62 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 35263.3 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 995.1 | |
| All* | Total formula weight | 36258.4 |
