MolNFT v1 · #83779 · protein
Crystal structure analysis of cell division protein
3WT0 · Cell division protein ftsa: “Crystal structure analysis of cell division protein”. X-ray diffraction, 2 ligands (ATP, MG), 20 pockets (best druggability 0.73). MolNFT v1 #83779 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 3WT0
- Type
- protein
- Length
- 1,504 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein ftsa
- UniProt
- Q8NX33
- Ligands
- ATP, MG
- Pockets
- 20 · best druggability 0.73
Structure
x-ray diffraction · 3 distinct chains · 38% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cell division protein ftsa | protein | 376 | 38% helix, 34% strand | Q8NX33 |
| C | Cell division protein ftsa | protein | 374 | 38% helix, 34% strand | Q8NX33 |
| D | Cell division protein ftsa | protein | 378 | 38% helix, 34% strand | Q8NX33 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 270 | 0.73 | 0.87 | 42 | ATP, MG |
| 2 | 241 | 0.72 | 0.88 | 39 | ATP, MG |
| 3 | 258 | 0.72 | 0.87 | 43 | ATP, MG |
| 4 | 336 | 0.71 | 0.84 | 44 | ATP, MG |
| 5 | 506 | 0.67 | 0.78 | 56 | empty |
Interfaces
3 interfaces between chains.
- A–C · 558 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 373 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 193 Ų buried · 1 hydrogen bond · 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 Q8NX33
- Elsewhere: RCSB PDB 3WT0 · PDBe 3WT0 · UniProt Q8NX33
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