MolNFT v1 · #25315 · 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, 2 pockets (best druggability 0.52). MolNFT v1 #25315 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1VLZ
- Type
- protein
- Length
- 255 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chey
- UniProt
- P06143
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 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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