Research workbench
The novel membrane-proximal sensing mechanism in a broad-ligand binding chemoreceptor mcpa of bacillus velezensis
Analyse The novel membrane-proximal sensing mechanism in a broad-ligand binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7W0W
- Type
- protein
- Length
- 285 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methyl-accepting chemotaxis protein
- UniProt
- A0A7U2PGC4
- Ligands
- LMR
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methyl-accepting chemotaxis protein | protein | 131 | 40% helix, 23% strand | A0A7U2PGC4 |
| B | Methyl-accepting chemotaxis protein | protein | 154 | 42% helix, 22% strand | A0A7U2PGC4 |
Ligands and binding sites
- LMR · (2S)-2-hydroxybutanedioic acid · ligand · 2 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 215 | 0.53 | 0.77 | 37 | empty |
Interfaces
1 interface between chains.
- A–B · 660 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 7W0W · The novel membrane-proximal sensing mechanism in a broad-ligand binding chemoreceptor… · 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 A0A7U2PGC4
- Elsewhere: RCSB PDB 7W0W · PDBe 7W0W · UniProt A0A7U2PGC4
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