Research workbench
Crysatl structure of a bacterial cell-surface flagellin N20C20
Analyse Crysatl structure of a bacterial cell-surface flagellin N20C20 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3K8V
- Type
- protein
- Length
- 643 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellin homolog
- UniProt
- Q2PHB2
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 56% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flagellin homolog | protein | 323 | 56% helix, 17% strand | Q2PHB2 |
| B | Flagellin homolog | protein | 320 | 55% helix, 18% strand | Q2PHB2 |
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 | 908 | 0.72 | 0.77 | 92 | empty |
| 2 | 115 | 0.43 | 0.77 | 22 | empty |
| 3 | 100 | 0.38 | 0.75 | 21 | empty |
| 4 | 83 | 0.33 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 878 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 3K8V · Crysatl structure of a bacterial cell-surface flagellin N20C20 · 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 Q2PHB2
- Elsewhere: RCSB PDB 3K8V · PDBe 3K8V · UniProt Q2PHB2
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