Research workbench
Crystal structure of the bacterial cell division protein ftsq and ftsb
Analyse Crystal structure of the bacterial cell division protein ftsq and ftsb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Z2W
- Type
- protein
- Length
- 244 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsq; Cell division protein ftsb
- UniProt
- J7Q602, A0A1Q6B6Y5
- Ligands
- MG
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein ftsq | protein | 209 | 27% helix, 30% strand | J7Q602 |
| B | Cell division protein ftsb | protein | 35 | 37% helix, 14% strand | A0A1Q6B6Y5 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 60 | 0.42 | 0.82 | 17 | empty |
| 2 | 54 | 0.41 | 0.81 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 964 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 5Z2W · Crystal structure of the bacterial cell division protein FtsQ and FtsB · the same entry in another collection · chain B against B, TM-score 1.00
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 J7Q602
- Every structure of UniProt A0A1Q6B6Y5
- Elsewhere: RCSB PDB 5Z2W · PDBe 5Z2W · UniProt J7Q602 · UniProt A0A1Q6B6Y5
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