MolNFT v1 · #51664 · protein
Xray structure of ftsk gamma domain (P. aeruginosa)
2VE8 · DNA translocase ftsk: “Xray structure of ftsk gamma domain (P. aeruginosa)”. X-ray diffraction, 4 pockets (best druggability 0.87). MolNFT v1 #51664 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2VE8
- Type
- protein
- Length
- 515 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA translocase ftsk
- UniProt
- Q9I0M3
- Pockets
- 4 · best druggability 0.87
Structure
x-ray diffraction · 8 distinct chains · 50% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA translocase ftsk | protein | 67 | 48% helix, 3% strand | Q9I0M3 |
| B | DNA translocase ftsk | protein | 65 | 49% helix, 3% strand | Q9I0M3 |
| C | DNA translocase ftsk | protein | 62 | 52% helix, 3% strand | Q9I0M3 |
| D | DNA translocase ftsk | protein | 68 | 47% helix, 3% strand | Q9I0M3 |
| E | DNA translocase ftsk | protein | 66 | 48% helix, 3% strand | Q9I0M3 |
| F | DNA translocase ftsk | protein | 65 | 49% helix, 3% strand | Q9I0M3 |
| G | DNA translocase ftsk | protein | 60 | 53% helix, 3% strand | Q9I0M3 |
| H | DNA translocase ftsk | protein | 62 | 52% helix, 3% strand | Q9I0M3 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1028 | 0.87 | 0.88 | 121 | empty |
| 2 | 116 | 0.76 | 0.96 | 33 | empty |
| 3 | 58 | 0.41 | 0.81 | 18 | empty |
| 4 | 61 | 0.35 | 0.78 | 15 | empty |
Interfaces
20 interfaces between chains.
- A–D · 455 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 438 Ų buried · 6 hydrogen bonds · protein-protein
- B–E · 435 Ų buried · 10 hydrogen bonds · protein-protein
- D–F · 418 Ų buried · 9 hydrogen bonds · protein-protein
- A–G · 400 Ų buried · 8 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 Q9I0M3
- Elsewhere: RCSB PDB 2VE8 · PDBe 2VE8 · UniProt Q9I0M3
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