Research workbench
C-terminal domain of the tssa component of the type VI secretion system from burkholderia cenocepacia
Analyse C-terminal domain of the tssa component of the type VI secretion system from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HS6
- Type
- protein
- Length
- 548 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Type VI secretion protein impa
- UniProt
- A0A1V2W6E8
- Pockets
- 2 · best druggability 0.31
Structure
x-ray diffraction · 4 distinct chains · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, G, F | Type VI secretion protein impa | protein | 69 | 71% helix, 0% strand | A0A1V2W6E8 |
| C, B | Type VI secretion protein impa | protein | 68 | 72% helix, 0% strand | A0A1V2W6E8 |
| H | Type VI secretion protein impa | protein | 69 | 80% helix, 0% strand | A0A1V2W6E8 |
| E, D | Type VI secretion protein impa | protein | 68 | 69% helix, 0% strand | A0A1V2W6E8 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.31 | 0.75 | 17 | empty |
| 2 | 61 | 0.28 | 0.74 | 12 | empty |
Interfaces
7 interfaces between chains.
- C–D · 490 Ų buried · 12 hydrogen bonds · protein-protein
- C–B · 470 Ų buried · 8 hydrogen bonds · protein-protein
- E–D · 462 Ų buried · 8 hydrogen bonds · protein-protein
- H–G · 461 Ų buried · 6 hydrogen bonds · protein-protein
- F–E · 460 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 6HS6 · C-terminal domain of the TssA component of the type VI secretion system from Burkholderia… · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A1V2W6E8
- Elsewhere: RCSB PDB 6HS6 · PDBe 6HS6 · UniProt A0A1V2W6E8
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