3G8D
Crystal structure of the biotin carboxylase subunit, E296A mutant, of acetyl-COA carboxylase from Escherichia coli
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B | Biotin carboxylase | polymer | 444 | 48772.0 | 2 | UniProt (P24182) Pfam (PF00289) Pfam (PF02786) Pfam (PF02785) In PDB | Escherichia coli | Acetyl-CoA carboxylase subunit A, ACC |
| 2 | A, B | SULFATE ION | non-polymer | 96.1 | 2 | Chemie (SO4) | |||
| 3 | B | ADENOSINE-5'-DIPHOSPHATE | non-polymer | 427.2 | 1 | Chemie (ADP) | |||
| 4 | B | MAGNESIUM ION | non-polymer | 24.3 | 1 | Chemie (MG) | |||
| 5 | water | water | 18.0 | 478 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 444 (UniProt: P24182)
| PDB | External Database | Details |
|---|---|---|
| Ala 296 | Glu 296 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 97544.0 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 643.6 | |
| All* | Total formula weight | 98187.6 |
