MolNFT v1 · #56959 · protein
Structure of the periplasmic domain of motb from salmonella (crystal form III)
2ZVZ · Chemotaxis protein motb: “Structure of the periplasmic domain of motb from salmonella (crystal form III)”. X-ray diffraction, 4 pockets (best druggability 0.74). MolNFT v1 #56959 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 2ZVZ
- Type
- protein
- Length
- 331 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chemotaxis protein motb
- UniProt
- P55892
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chemotaxis protein motb | protein | 170 | 41% helix, 21% strand | P55892 |
| B | Chemotaxis protein motb | protein | 161 | 45% helix, 22% strand | P55892 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 597 | 0.74 | 0.81 | 73 | empty |
| 2 | 95 | 0.38 | 0.76 | 21 | empty |
| 3 | 62 | 0.32 | 0.76 | 17 | empty |
| 4 | 55 | 0.26 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1123 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 2ZVZ · Structure of the periplasmic domain of MotB from Salmonella (crystal form III) · the same entry in another collection · chain A against A, TM-score 1.00
- P55892 · AlphaFold monomer V2.0 prediction for motility protein B (P55892) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P55892
- Elsewhere: RCSB PDB 2ZVZ · PDBe 2ZVZ · UniProt P55892
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