Research workbench
Uncoupled phosphorylation and activation in bacterial chemotaxis: the 2.1 ångström structure of a threonine to isoleucine mutant at position 87 of chey
Analyse Uncoupled phosphorylation and activation in bacterial chemotaxis: the 2.1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VLZ
- Type
- protein
- Length
- 255 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.05
- Source
- Escherichia coli
- Molecule
- Chey
- UniProt
- P06143
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · resolution 2.05 · 2 distinct chains · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chey | protein | 128 | 43% helix, 17% strand | P06143 |
| B | Chey | protein | 127 | 47% helix, 17% strand | P06143 |
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 | 259 | 0.52 | 0.75 | 23 | empty |
| 2 | 87 | 0.41 | 0.78 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 441 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1VLZ · Uncoupled phosphorylation and activation in bacterial chemotaxis: the 2.1 ångström… · the same entry in another collection · chain A against A, TM-score 1.00
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 P06143
- Elsewhere: RCSB PDB 1VLZ · PDBe 1VLZ · UniProt P06143
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