Research workbench
Structure of FTSY:GMPPNP complex
Analyse Structure of FTSY:GMPPNP complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q9B
- Type
- protein
- Length
- 590 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsy
- UniProt
- P83749
- Ligands
- GNP, SO4
- Pockets
- 12 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein ftsy | protein | 303 | 52% helix, 12% strand | P83749 |
| B | Cell division protein ftsy | protein | 287 | 50% helix, 12% strand | P83749 |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
- SO4 · Sulfate ion · ion · 8 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 | 561 | 0.76 | 0.83 | 47 | SO4 |
| 2 | 498 | 0.69 | 0.80 | 50 | SO4, EDO |
| 3 | 179 | 0.69 | 0.87 | 28 | empty |
| 4 | 200 | 0.54 | 0.79 | 33 | GNP |
| 5 | 70 | 0.50 | 0.85 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1089 Ų buried · 12 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 2Q9B · PDBe 2Q9B · UniProt P83749
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