Research workbench
Structure of apo ftsy
Analyse Structure of apo ftsy in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q9A
- Type
- protein
- Length
- 594 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsy
- UniProt
- P83749
- Ligands
- SO4
- Pockets
- 12 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein ftsy | protein | 304 | 50% helix, 12% strand | P83749 |
| B | Cell division protein ftsy | protein | 290 | 49% helix, 12% strand | P83749 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 9 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 9 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 517 | 0.75 | 0.83 | 52 | SO4 |
| 2 | 477 | 0.68 | 0.80 | 56 | SO4, EDO |
| 3 | 73 | 0.59 | 0.89 | 20 | empty |
| 4 | 232 | 0.58 | 0.79 | 36 | SO4 |
| 5 | 230 | 0.55 | 0.78 | 33 | SO4 |
Interfaces
1 interface between chains.
- A–B · 1109 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
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 P83749
- Elsewhere: RCSB PDB 2Q9A · PDBe 2Q9A · UniProt P83749
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