Research workbench
Crystal structure of an E.COLI phoq sensor domain mutant
Analyse Crystal structure of an E.COLI phoq sensor domain mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BQA
- Type
- protein
- Length
- 292 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
- SO4
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sensor protein phoq (EC 2.7.13.3) | protein | 146 | 36% helix, 27% strand | P23837 |
| B | Sensor protein phoq (EC 2.7.13.3) | protein | 146 | 33% helix, 32% strand | P23837 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 97 | 0.57 | 0.86 | 24 | empty |
| 2 | 148 | 0.56 | 0.82 | 23 | empty |
| 3 | 102 | 0.39 | 0.76 | 14 | SO4 |
| 4 | 69 | 0.38 | 0.79 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1308 Ų buried · 10 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 P23837
- Elsewhere: RCSB PDB 3BQA · PDBe 3BQA · UniProt P23837
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