Research workbench
The dynamic dimer structure of the chaperone trigger factor (conformer 1)
Analyse The dynamic dimer structure of the chaperone trigger factor (conformer 1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OWI
- Type
- protein
- Length
- 864 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trigger factor
- EC
- 5.2.1.8
- UniProt
- P0A850
- Pockets
- 17 · best druggability 0.81
Structure
solution nmr · 1 distinct chain · 46% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Trigger factor (EC 5.2.1.8) | protein | 432 | 46% helix, 13% strand | P0A850 |
Pockets
17 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 792 | 0.81 | 0.84 | 90 | empty |
| 2 | 486 | 0.77 | 0.84 | 55 | empty |
| 3 | 255 | 0.71 | 0.85 | 28 | empty |
| 4 | 356 | 0.70 | 0.83 | 48 | empty |
| 5 | 323 | 0.70 | 0.83 | 43 | empty |
Interfaces
1 interface between chains.
- A–B · 2456 Ų buried · 29 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 P0A850
- Elsewhere: RCSB PDB 5OWI · PDBe 5OWI · UniProt P0A850
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