Research workbench
Cryo-EM structure of the flagellar MS ring with FlgB-Dc loop and FliE-helix 1 from Salmonella
Analyse Cryo-EM structure of the flagellar MS ring with FlgB-Dc loop and FliE-helix 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E81
- Type
- protein
- Length
- 7,551 residues
- Chains
- 68
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 4.5
- Source
- Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
- Molecule
- Flagellar M-ring protein; FlgB-Dc loop; FliE helix 1
- UniProt
- P15928
- Pockets
- 20 · best druggability 0.81
Structure
electron microscopy · resolution 4.5 · 11 distinct chains · 31% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| Da, Db, Dc, Dd, Dp, Dq, Dr, Ds, Dt, Du, Dv, Dw | Flagellar M-ring protein | protein | 109 | 29% helix, 14% strand | P15928 |
| De | Flagellar M-ring protein | protein | 99 | 32% helix, 15% strand | P15928 |
| Df, Do | Flagellar M-ring protein | protein | 97 | 29% helix, 15% strand | P15928 |
| Dg, Dh, Di, Dj, Dk, Dl, Dm, Dn | Flagellar M-ring protein | protein | 87 | 32% helix, 17% strand | P15928 |
| GA, GC | FlgB-Dc loop | protein | 11 | 0% helix, 0% strand | — |
| GF, GG, GH, GJ, GK | FliE helix 1 | protein | 18 | 89% helix, 0% strand | — |
| GI | FliE helix 1 | protein | 15 | 87% helix, 0% strand | — |
| GE | FlgB-Dc loop | protein | 12 | 0% helix, 0% strand | — |
| GD | FlgB-Dc loop | protein | 10 | 0% helix, 0% strand | — |
| GB | FlgB-Dc loop | protein | 5 | 0% helix, 0% strand | — |
| Ca, Cb, Cc, Cd, Ce, Cf, cg, Ch, Ci, Cj, Ck, Cl, Cm, Cn, Co, Cp, Cq, Cr, Cs, Ct, Cu, Cv, Cw, Cx, Cy, Cz, Ea, Eb, Ec, Ed, Ee, Ef, Eg, Fh | Flagellar M-ring protein | protein | 150 | 26% helix, 36% strand | P15928 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 927 | 0.81 | 0.82 | 128 | empty |
| 2 | 770 | 0.76 | 0.81 | 89 | empty |
| 3 | 388 | 0.73 | 0.84 | 31 | empty |
| 4 | 400 | 0.73 | 0.84 | 38 | empty |
| 5 | 378 | 0.73 | 0.84 | 36 | empty |
Interfaces
108 interfaces between chains.
- Eg–Fh · 2270 Ų buried · 37 hydrogen bonds · protein-protein
- Cq–Cr · 2268 Ų buried · 36 hydrogen bonds · protein-protein
- Cn–Co · 2267 Ų buried · 34 hydrogen bonds · protein-protein
- Ch–Ci · 2266 Ų buried · 36 hydrogen bonds · protein-protein
- Co–Cp · 2266 Ų buried · 37 hydrogen bonds · protein-protein
Compared structures
- P15928 · AlphaFold monomer V2.0 prediction for flagellar M-ring protein (P15928) · a predicted model of the same protein · chain Dl 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 P15928
- Elsewhere: RCSB PDB 7E81 · PDBe 7E81 · UniProt P15928
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