Research workbench
Ceue (H227A variant) a periplasmic protein from campylobacter jejuni
Analyse Ceue (H227A 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
- 5MBQ
- Type
- protein
- Length
- 853 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enterochelin uptake periplasmic binding protein
- UniProt
- Q0P8Q4
- Pockets
- 8 · best druggability 0.67
Structure
x-ray diffraction · 3 distinct chains · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enterochelin uptake periplasmic binding protein | protein | 286 | 40% helix, 21% strand | Q0P8Q4 |
| B | Enterochelin uptake periplasmic binding protein | protein | 285 | 41% helix, 21% strand | Q0P8Q4 |
| C | Enterochelin uptake periplasmic binding protein | protein | 282 | 43% helix, 21% strand | Q0P8Q4 |
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 453 | 0.67 | 0.79 | 62 | empty |
| 2 | 305 | 0.65 | 0.81 | 48 | empty |
| 3 | 432 | 0.63 | 0.77 | 51 | empty |
| 4 | 281 | 0.61 | 0.80 | 42 | empty |
| 5 | 347 | 0.60 | 0.77 | 33 | empty |
Interfaces
3 interfaces between chains.
- A–C · 524 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 419 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 330 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 5MBQ · CeuE (H227A 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 5MBQ · PDBe 5MBQ · UniProt Q0P8Q4
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