Research workbench
CeuE (H227L, Y288F variant) a periplasmic protein from Campylobacter jejuni
Analyse CeuE (H227L, Y288F variant) a periplasmic protein from Campylobacter jejuni in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MBT
- Type
- protein
- Length
- 848 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Campylobacter jejuni
- Molecule
- Enterochelin uptake periplasmic binding protein
- UniProt
- Q0P8Q4
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · resolution 1.8 · 3 distinct chains · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enterochelin uptake periplasmic binding protein | protein | 282 | 40% helix, 20% strand | Q0P8Q4 |
| B | Enterochelin uptake periplasmic binding protein | protein | 284 | 41% helix, 21% strand | Q0P8Q4 |
| C | Enterochelin uptake periplasmic binding protein | protein | 282 | 41% helix, 22% strand | Q0P8Q4 |
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1132 | 0.73 | 0.76 | 105 | empty |
| 2 | 525 | 0.73 | 0.81 | 63 | empty |
| 3 | 474 | 0.67 | 0.79 | 58 | empty |
| 4 | 254 | 0.65 | 0.82 | 39 | empty |
| 5 | 66 | 0.38 | 0.79 | 19 | empty |
Interfaces
3 interfaces between chains.
- B–C · 615 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 512 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 308 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 5MBT · Ceue (H227L, Y288F variant) a periplasmic protein from campylobacter jejuni · 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 Q0P8Q4
- Elsewhere: RCSB PDB 5MBT · PDBe 5MBT · UniProt Q0P8Q4
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