Research workbench
the competence regulator ComR from Streptococcus vestibularis in complex with its cognate signaling peptide XIP
Analyse the competence regulator ComR from Streptococcus vestibularis in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HUA
- Type
- protein
- Length
- 541 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.389
- Source
- Streptococcus vestibularis F0396
- Molecule
- Uncharacterized protein; XIP signaling peptide
- UniProt
- E3CNF6
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · resolution 3.389 · 3 distinct chains · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 296 | 69% helix, 0% strand | E3CNF6 |
| B | Uncharacterized protein | protein | 229 | 69% helix, 0% strand | E3CNF6 |
| C, D | XIP signaling peptide | protein | 8 | 38% helix, 0% strand | — |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 213 | 0.64 | 0.83 | 25 | empty |
| 2 | 226 | 0.53 | 0.77 | 28 | empty |
| 3 | 147 | 0.51 | 0.79 | 21 | empty |
| 4 | 119 | 0.42 | 0.76 | 20 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1034 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 942 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 925 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 6HUA · The competence regulator comr from streptococcus vestibularis in complex with its cognate… · 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 E3CNF6
- Elsewhere: RCSB PDB 6HUA · PDBe 6HUA · UniProt E3CNF6
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