9KKM
cryo-EM structure of acetyl-CoA carboxyltransferase holoenzyme dimer from Shewanella oneidensis, mutant E1238A, complexed with ADP
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B (A, B) | Acetyl-CoA carboxylase multifunctional enzyme AccADCB | polymer | 1517 | 167752.1 | 2 | UniProt (Q8EIJ9) Pfam (PF03255) Pfam (PF00289) Pfam (PF02786) Pfam (PF02785) | Shewanella oneidensis MR-1 | acetyl-CoA carboxyltransferase |
| 2 | C, E (A, B) | ADENOSINE-5'-DIPHOSPHATE | non-polymer | 427.2 | 2 | Chemie (ADP) | |||
| 3 | D, F (A, B) | MAGNESIUM ION | non-polymer | 24.3 | 2 | Chemie (MG) |
Sequence modifications
A, B: 1 - 1517 (UniProt: Q8EIJ9)
| PDB | External Database | Details |
|---|---|---|
| Ala 1238 | Glu 1238 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 335504.2 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 903.0 | |
| All* | Total formula weight | 336407.2 |
