Research workbench
Crystal structure of the flagellar cap protein flid from helicobacter pylori
Analyse Crystal structure of the flagellar cap protein flid from helicobacter pylori in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IWY
- Type
- protein
- Length
- 366 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar hook-associated protein 2
- UniProt
- P96786
- Pockets
- 2 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flagellar hook-associated protein 2 | protein | 366 | 19% helix, 38% strand | P96786 |
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 | 336 | 0.60 | 0.78 | 55 | empty |
| 2 | 55 | 0.33 | 0.77 | 12 | empty |
Compared structures
- 6IWY · Crystal structure of the flagellar cap protein FliD from Helicobacter pylori · the same entry in another collection · chain A against A, TM-score 1.00
- P96786 · AlphaFold monomer V2.0 prediction for flagellar hook-associated protein 2 (P96786) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P96786
- Elsewhere: RCSB PDB 6IWY · PDBe 6IWY · UniProt P96786
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