Research workbench
Cryo-EM structure of the flagellar ms ring with C34 symmetry from salmonella
Analyse Cryo-EM structure of the flagellar ms ring with C34 symmetry from salmonella in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CG7
- Type
- protein
- Length
- 5,100 residues
- Chains
- 34
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar M-ring protein
- UniProt
- P15928
- Pockets
- 20 · best druggability 0.73
Structure
electron microscopy · 1 distinct chain · 26% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, c, b, d, e, f, g, h | 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 | 388 | 0.73 | 0.84 | 31 | empty |
| 2 | 400 | 0.73 | 0.84 | 38 | empty |
| 3 | 378 | 0.73 | 0.84 | 36 | empty |
| 4 | 377 | 0.73 | 0.84 | 38 | empty |
| 5 | 389 | 0.73 | 0.84 | 36 | empty |
Interfaces
34 interfaces between chains.
- g–h · 2269 Ų buried · 37 hydrogen bonds · protein-protein
- e–f · 2267 Ų buried · 37 hydrogen bonds · protein-protein
- H–I · 2266 Ų buried · 36 hydrogen bonds · protein-protein
- N–O · 2266 Ų buried · 34 hydrogen bonds · protein-protein
- O–P · 2265 Ų buried · 37 hydrogen bonds · protein-protein
Compared structures
- 7CG7 · Cryo-EM structure of the flagellar MS ring with C34 symmetry from Salmonella · the same entry in another collection · chain B against B, 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 P15928
- Elsewhere: RCSB PDB 7CG7 · PDBe 7CG7 · UniProt P15928
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.