Research workbench
Staphylococcus aureus ftsa complexed with amppnp
Analyse Staphylococcus aureus ftsa complexed with amppnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WQT
- Type
- protein
- Length
- 1,424 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsa
- UniProt
- Q6GHQ0
- Ligands
- ANP, MG, CL
- Pockets
- 18 · best druggability 0.76
Structure
x-ray diffraction · 4 distinct chains · 37% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein ftsa | protein | 370 | 37% helix, 35% strand | Q6GHQ0 |
| B | Cell division protein ftsa | protein | 334 | 38% helix, 32% strand | Q6GHQ0 |
| C | Cell division protein ftsa | protein | 368 | 38% helix, 35% strand | Q6GHQ0 |
| D | Cell division protein ftsa | protein | 352 | 36% helix, 34% strand | Q6GHQ0 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 6 copies · chains A, B, C, D
- CL · Chloride ion · ion · 9 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 483 | 0.76 | 0.84 | 63 | empty |
| 2 | 211 | 0.74 | 0.90 | 38 | MG, ANP |
| 3 | 830 | 0.74 | 0.79 | 71 | empty |
| 4 | 251 | 0.72 | 0.87 | 39 | MG, ANP |
| 5 | 261 | 0.72 | 0.87 | 39 | MG, ANP |
Interfaces
5 interfaces between chains.
- A–B · 891 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 782 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 751 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 494 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 220 Ų buried · 3 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 Q6GHQ0
- Elsewhere: RCSB PDB 3WQT · PDBe 3WQT · UniProt Q6GHQ0
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