Research workbench
The bacterial cell-division protein zipa and its interaction with an ftsz fragment revealed by X-ray crystallography
Analyse The bacterial cell-division protein zipa and its interaction with an ftsz… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F47
- Type
- protein
- Length
- 161 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein zipa; Cell division protein ftsz
- UniProt
- P77173, P0A9A6
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Cell division protein zipa | protein | 144 | 34% helix, 27% strand | P77173 |
| A | Cell division protein ftsz | protein | 17 | 53% helix, 6% strand | P0A9A6 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.38 | 0.78 | 18 | empty |
| 2 | 68 | 0.29 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- B–A · 583 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1F47 · The bacterial cell-division protein zipa and its interaction with an ftsz fragment… · the same entry in another collection · chain B against B, TM-score 1.00
- P77173 · AlphaFold monomer V2.0 prediction for cell division protein zipa (P77173) · a predicted model of the same protein · chain B against A, TM-score 0.97
- P0A9A6 · AlphaFold monomer V2.0 prediction for cell division protein ftsz (P0A9A6) · a predicted model of the same protein · chain A against A, TM-score 0.49
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P77173
- Every structure of UniProt P0A9A6
- Elsewhere: RCSB PDB 1F47 · PDBe 1F47 · UniProt P77173 · UniProt P0A9A6
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