Research workbench
Osmoporin (OMPK36) from klebsiella pneumoniae
Analyse Osmoporin (OMPK36) from klebsiella pneumoniae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OSM
- Type
- protein
- Length
- 1,026 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- OMPK36
- UniProt
- Q48473
- Ligands
- D12
- Pockets
- 10 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | OMPK36 | protein | 342 | 7% helix, 57% strand | Q48473 |
Ligands and binding sites
- D12 · Dodecane · ligand · 9 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 212 | 0.77 | 0.92 | 49 | empty |
| 2 | 83 | 0.75 | 0.96 | 21 | empty |
| 3 | 1038 | 0.70 | 0.75 | 75 | empty |
| 4 | 969 | 0.70 | 0.74 | 71 | empty |
| 5 | 659 | 0.68 | 0.77 | 60 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1654 Ų buried · 24 hydrogen bonds · protein-protein
- B–C · 1645 Ų buried · 26 hydrogen bonds · protein-protein
- A–B · 1644 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
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 Q48473
- Elsewhere: RCSB PDB 1OSM · PDBe 1OSM · UniProt Q48473
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