3R9I
2.6A resolution structure of MinD complexed with MinE (12-31) peptide
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 (A, B, C, D) | Septum site-determining protein minD | polymer | 260 | 28500.7 | 4 | UniProt (P0AEZ3) Pfam (PF01656) | Escherichia coli | Cell division inhibitor minD |
| 2 | E, F, G, H (E, F, G, H) | Cell division topological specificity factor | polymer | 20 | 2385.8 | 4 | UniProt (P0A734) | Escherichia coli | minE |
| 3 | I, J, K, L (A, B, C, D) | ADENOSINE-5'-DIPHOSPHATE | non-polymer | 427.2 | 4 | Chemie (ADP) | |||
| 4 | M, N, O, P, Q... (A, B, C, D, E...) | water | water | 18.0 | 177 | Chemie (HOH) |
Sequence modifications
A, B, C, D: 1 - 260 (UniProt: P0AEZ3)
| PDB | External Database | Details |
|---|---|---|
| Ala 40 | Asp 40 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 8 |
| Total formula weight | 123545.9 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 1708.8 | |
| All* | Total formula weight | 125254.7 |
