Research workbench
Crystal structure of Omp36 from Enterobacter aerogenes
Analyse Crystal structure of Omp36 from Enterobacter aerogenes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5O9C
- Type
- protein
- Length
- 1,392 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.469
- Source
- Klebsiella aerogenes
- Molecule
- Osmoporin Omp36
- UniProt
- Q9ALY0
- Pockets
- 13 · best druggability 0.73
Structure
x-ray diffraction · resolution 2.469 · 1 distinct chain · 9% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, A, D, B | Osmoporin Omp36 | protein | 348 | 9% helix, 56% strand | Q9ALY0 |
Ligands and binding sites
- C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 4 copies · chains A, D, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 747 | 0.73 | 0.78 | 60 | empty |
| 2 | 654 | 0.72 | 0.78 | 58 | empty |
| 3 | 962 | 0.70 | 0.75 | 63 | empty |
| 4 | 992 | 0.70 | 0.75 | 70 | C8E |
| 5 | 959 | 0.70 | 0.75 | 68 | C8E |
Interfaces
4 interfaces between chains.
- C–B · 642 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 431 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 285 Ų buried · 6 hydrogen bonds · protein-protein
- C–A · 126 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 5O9C · Crystal structure of OMP36 from enterobacter aerogenes · 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 Q9ALY0
- Elsewhere: RCSB PDB 5O9C · PDBe 5O9C · UniProt Q9ALY0
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