Research workbench
Crystal structure of periplasmic domain of helicobacter pylori flil (residues 81 to 183) (crystal form B)
Analyse Crystal structure of periplasmic domain of helicobacter pylori flil (residues… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7SGO
- Type
- protein
- Length
- 605 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar protein flil
- UniProt
- A0A293T1P9
- Pockets
- 5 · best druggability 0.49
Structure
x-ray diffraction · 3 distinct chains · 39% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Flagellar protein flil | protein | 102 | 38% helix, 29% strand | A0A293T1P9 |
| B, E, F | Flagellar protein flil | protein | 100 | 40% helix, 30% strand | A0A293T1P9 |
| C | Flagellar protein flil | protein | 101 | 39% helix, 30% strand | A0A293T1P9 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 271 | 0.49 | 0.73 | 40 | empty |
| 2 | 209 | 0.45 | 0.73 | 28 | empty |
| 3 | 98 | 0.39 | 0.76 | 20 | empty |
| 4 | 118 | 0.39 | 0.74 | 14 | empty |
| 5 | 52 | 0.35 | 0.79 | 18 | empty |
Interfaces
6 interfaces between chains.
- C–F · 681 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 662 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 625 Ų buried · 9 hydrogen bonds · protein-protein
- B–E · 343 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 308 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 7SGO · Crystal structure of periplasmic domain of Helicobacter pylori FliL (residues 81 to 183)… · 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 A0A293T1P9
- Elsewhere: RCSB PDB 7SGO · PDBe 7SGO · UniProt A0A293T1P9
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