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Crystal structure of the E.COLI phoq sensor domain
Analyse Crystal structure of the E.COLI phoq sensor domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BQ8
- Type
- protein
- Length
- 275 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sensor protein phoq
- EC
- 2.7.13.3
- UniProt
- P23837
- Ligands
- NI
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sensor protein phoq (EC 2.7.13.3) | protein | 142 | 36% helix, 30% strand | P23837 |
| B | Sensor protein phoq (EC 2.7.13.3) | protein | 133 | 33% helix, 32% strand | P23837 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 205 | 0.52 | 0.77 | 26 | empty |
| 2 | 112 | 0.42 | 0.77 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 844 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 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 P23837
- Elsewhere: RCSB PDB 3BQ8 · PDBe 3BQ8 · UniProt P23837
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