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Crystal structure of E. COLI osmc
Analyse Crystal structure of E. COLI osmc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QWI
- Type
- protein
- Length
- 568 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Osmotically inducible protein
- UniProt
- P0C0L2
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Osmotically inducible protein | protein | 142 | 33% helix, 39% strand | P0C0L2 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1088 | 0.75 | 0.78 | 105 | empty |
| 2 | 110 | 0.46 | 0.78 | 19 | empty |
| 3 | 114 | 0.45 | 0.78 | 21 | empty |
| 4 | 156 | 0.42 | 0.74 | 22 | empty |
Interfaces
6 interfaces between chains.
- A–B · 3055 Ų buried · 54 hydrogen bonds · protein-protein
- C–D · 3054 Ų buried · 54 hydrogen bonds · protein-protein
- A–C · 166 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 156 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 80 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
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 P0C0L2
- Elsewhere: RCSB PDB 1QWI · PDBe 1QWI · UniProt P0C0L2
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