MolNFT v2 · #25321 · protein
Uncoupled phosphorylation and activation in bacterial chemotaxis: the 2.1 ångström structure of a threonine to isoleucine mutant at position 87 of chey
1VLZ: “Uncoupled phosphorylation and activation in bacterial chemotaxis: the 2.1 ångström structure of a threonine…”. X-ray diffraction at 2.05. MolNFT v2 #25321 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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
- UniProt
- P06143
Structure
x-ray diffraction · resolution 2.05 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 128 | — | P06143 |
| B | — | protein | 127 | — | P06143 |
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
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.