Research workbench
Structure of flis chaperone in complex with flagellin and HP1076
Analyse Structure of flis chaperone in complex with flagellin and HP1076 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LEA
- Type
- protein
- Length
- 537 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar secretion chaperone flis; Uncharacterized protein HP_1076; Flagellin
- UniProt
- I9NY49, O25709, A0A1Q2QRN0
- Pockets
- 3 · best druggability 0.59
Structure
x-ray diffraction · 4 distinct chains · 72% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Flagellar secretion chaperone flis | protein | 105 | 84% helix, 0% strand | I9NY49 |
| C | Uncharacterized protein HP_1076 | protein | 126 | 69% helix, 10% strand | O25709 |
| D | Uncharacterized protein HP_1076 | protein | 123 | 67% helix, 11% strand | O25709 |
| E, F | Flagellin | protein | 39 | 62% helix, 0% strand | A0A1Q2QRN0 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 344 | 0.59 | 0.76 | 39 | empty |
| 2 | 103 | 0.38 | 0.75 | 16 | empty |
| 3 | 53 | 0.28 | 0.74 | 13 | empty |
Interfaces
8 interfaces between chains.
- A–E · 1623 Ų buried · 12 hydrogen bonds · protein-protein
- B–F · 1623 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 974 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 957 Ų buried · 13 hydrogen bonds · protein-protein
- E–F · 286 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6LEA · Structure of FliS chaperone in complex with flagellin and HP1076 · 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 I9NY49
- Every structure of UniProt O25709
- Every structure of UniProt A0A1Q2QRN0
- Elsewhere: RCSB PDB 6LEA · PDBe 6LEA · UniProt I9NY49 · UniProt O25709 · UniProt A0A1Q2QRN0
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