Research workbench
Structure of the flipqr complex from the flagellar type 3 secretion system of vibrio mimicus.
Analyse Structure of the flipqr complex from the flagellar type 3 secretion system of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6S3S
- Type
- protein
- Length
- 1,569 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar biosynthetic protein flip; Flagellar biosynthetic protein flir; Flagellar…
- UniProt
- A0A2J9UXT5, A0A1D8S9I5, A0A1D8S9F5
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 7 distinct chains · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flagellar biosynthetic protein flip | protein | 191 | 73% helix, 0% strand | A0A2J9UXT5 |
| B | Flagellar biosynthetic protein flip | protein | 195 | 74% helix, 0% strand | A0A2J9UXT5 |
| C, D | Flagellar biosynthetic protein flip | protein | 196 | 68% helix, 0% strand | A0A2J9UXT5 |
| E | Flagellar biosynthetic protein flip | protein | 187 | 74% helix, 0% strand | A0A2J9UXT5 |
| F | Flagellar biosynthetic protein flir | protein | 257 | 68% helix, 0% strand | A0A1D8S9I5 |
| G, H, I | Flagellar biosynthetic protein fliq | protein | 89 | 85% helix, 0% strand | A0A1D8S9F5 |
| J | Flagellar biosynthetic protein fliq | protein | 80 | 90% helix, 0% strand | A0A1D8S9F5 |
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 233 | 0.85 | 0.96 | 36 | empty |
| 2 | 205 | 0.83 | 0.96 | 37 | empty |
| 3 | 182 | 0.83 | 0.96 | 39 | empty |
| 4 | 1134 | 0.77 | 0.79 | 91 | empty |
| 5 | 603 | 0.77 | 0.83 | 71 | empty |
Interfaces
28 interfaces between chains.
- E–F · 2131 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 2052 Ų buried · 2 hydrogen bonds · protein-protein
- A–F · 2045 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 1988 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 1961 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6S3S · Structure of the FliPQR complex from the flagellar type 3 secretion system of Vibrio… · 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 A0A2J9UXT5
- Every structure of UniProt A0A1D8S9I5
- Every structure of UniProt A0A1D8S9F5
- Elsewhere: RCSB PDB 6S3S · PDBe 6S3S · UniProt A0A2J9UXT5 · UniProt A0A1D8S9I5 · UniProt A0A1D8S9F5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.