MolNFT v1 · #81507 · protein
Crystal structure of flig (residues 86-343) from H. pylori
3USW · Flagellar motor switch protein: “Crystal structure of flig (residues 86-343) from H. pylori”. X-ray diffraction, 2 pockets (best druggability 0.52). MolNFT v1 #81507 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3USW
- Type
- protein
- Length
- 212 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar motor switch protein
- UniProt
- O25119
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flagellar motor switch protein | protein | 212 | 74% helix, 0% strand | O25119 |
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 | 212 | 0.52 | 0.77 | 19 | empty |
| 2 | 65 | 0.35 | 0.77 | 16 | empty |
Compared structures
- 3USW · Crystal structure of FliG (residues 86-343) from H. pylori · the same entry in another collection · chain A against A, TM-score 1.00
- O25119 · AlphaFold monomer V2.0 prediction for flagellar motor switch protein flig (O25119) · a predicted model of the same protein · chain A against A, TM-score 0.49
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 O25119
- Elsewhere: RCSB PDB 3USW · PDBe 3USW · UniProt O25119
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