Research workbench
Outer membrane protein ompw
Analyse Outer membrane protein ompw in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F1V
- Type
- protein
- Length
- 1,092 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Outer membrane protein W
- UniProt
- P0A915
- Pockets
- 15 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 69% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Outer membrane protein W | protein | 182 | 3% helix, 69% strand | P0A915 |
Ligands and binding sites
- GOL · Glycerol · additive · 6 copies · chains A, F, E, C, D, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1076 | 0.86 | 0.87 | 86 | empty |
| 2 | 1178 | 0.86 | 0.86 | 93 | empty |
| 3 | 863 | 0.79 | 0.83 | 86 | empty |
| 4 | 835 | 0.79 | 0.83 | 90 | empty |
| 5 | 101 | 0.50 | 0.81 | 20 | empty |
Interfaces
9 interfaces between chains.
- B–C · 734 Ų buried · 2 hydrogen bonds · protein-protein
- C–E · 682 Ų buried · 13 hydrogen bonds · protein-protein
- A–F · 681 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 672 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 670 Ų buried · 11 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 P0A915
- Elsewhere: RCSB PDB 2F1V · PDBe 2F1V · UniProt P0A915
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