Research workbench
Crystal structure of the flagellin-flis complex from bacillus subtilis
Analyse Crystal structure of the flagellin-flis complex from bacillus subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MAW
- Type
- protein
- Length
- 372 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellin; Flagellar protein flis
- UniProt
- P02968, P39739
- Pockets
- 5 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 70% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | Flagellin | protein | 260 | 65% helix, 8% strand | P02968 |
| E | Flagellar protein flis | protein | 112 | 83% helix, 0% strand | P39739 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.65 | 0.94 | 17 | empty |
| 2 | 166 | 0.45 | 0.75 | 21 | empty |
| 3 | 75 | 0.31 | 0.74 | 15 | empty |
| 4 | 61 | 0.30 | 0.75 | 13 | empty |
| 5 | 52 | 0.26 | 0.74 | 12 | empty |
Interfaces
1 interface between chains.
- D–E · 2541 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 5MAW · Crystal structure of the flagellin-FliS complex from Bacillus subtilis · the same entry in another collection · chain D against D, TM-score 1.00
- P39739 · AlphaFold monomer V2.0 prediction for flagellar secretion chaperone flis (P39739) · a predicted model of the same protein · chain E against A, TM-score 0.98
- P02968 · AlphaFold monomer V2.0 prediction for flagellin (P02968) · a predicted model of the same protein · chain D against A, TM-score 0.78
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 P02968
- Every structure of UniProt P39739
- Elsewhere: RCSB PDB 5MAW · PDBe 5MAW · UniProt P02968 · UniProt P39739
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