Research workbench
Stalled ftsk motor domain bound to dsdna end
Analyse Stalled ftsk motor domain bound to dsdna end in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6T8O
- Type
- protein + DNA
- Length
- 2,400 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA translocase ftsk; Dsdna substrate
- UniProt
- Q9I0M3
- Ligands
- ADP
- Pockets
- 20 · best druggability 0.80
Structure
electron microscopy · 8 distinct chains · 36% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA translocase ftsk | protein | 395 | 35% helix, 18% strand | Q9I0M3 |
| B | DNA translocase ftsk | protein | 392 | 36% helix, 17% strand | Q9I0M3 |
| C | DNA translocase ftsk | protein | 398 | 35% helix, 19% strand | Q9I0M3 |
| D | DNA translocase ftsk | protein | 396 | 37% helix, 19% strand | Q9I0M3 |
| E | DNA translocase ftsk | protein | 396 | 34% helix, 18% strand | Q9I0M3 |
| F | DNA translocase ftsk | protein | 397 | 38% helix, 17% strand | Q9I0M3 |
| G | Dsdna substrate | dna | 13 | — | — |
| H | Dsdna substrate | dna | 13 | — | — |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 865 | 0.80 | 0.83 | 102 | empty |
| 2 | 892 | 0.76 | 0.80 | 75 | empty |
| 3 | 480 | 0.75 | 0.84 | 53 | empty |
| 4 | 430 | 0.73 | 0.83 | 66 | empty |
| 5 | 685 | 0.70 | 0.78 | 74 | ADP |
Interfaces
17 interfaces between chains.
- A–F · 1374 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 1178 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 1157 Ų buried · 8 hydrogen bonds · protein-protein
- D–E · 1119 Ų buried · 6 hydrogen bonds · protein-protein
- E–F · 1109 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 6T8O · PDBe 6T8O · UniProt Q9I0M3
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