Research workbench
Crystal structure of flig-flim complex from H. pylori
Analyse Crystal structure of flig-flim complex from H. pylori in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FQ0
- Type
- protein
- Length
- 522 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar motor switch protein
- UniProt
- O25675, O25119
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 44% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Flagellar motor switch protein | protein | 182 | 40% helix, 32% strand | O25675 |
| A | Flagellar motor switch protein | protein | 180 | 38% helix, 29% strand | O25675 |
| C, D | Flagellar motor switch protein | protein | 80 | 69% helix, 0% strand | O25119 |
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 | 371 | 0.80 | 0.89 | 52 | empty |
| 2 | 104 | 0.36 | 0.74 | 17 | empty |
| 3 | 90 | 0.35 | 0.75 | 17 | empty |
Interfaces
5 interfaces between chains.
- B–A · 1060 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 862 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 841 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 27 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 25 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4FQ0 · Crystal structure of FliG-FliM complex from H. pylori · the same entry in another collection · chain B against B, TM-score 1.00
- O25119 · AlphaFold monomer V2.0 prediction for flagellar motor switch protein flig (O25119) · a predicted model of the same protein · chain C against A, TM-score 0.96
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 O25675
- Every structure of UniProt O25119
- Elsewhere: RCSB PDB 4FQ0 · PDBe 4FQ0 · UniProt O25675 · UniProt O25119
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.