Research workbench
Cryo-EM structure of B. subtilis flagellar filaments N226Y
Analyse Cryo-EM structure of B. subtilis flagellar filaments N226Y in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WJT
- Type
- protein
- Length
- 12,382 residues
- Chains
- 41
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellin
- UniProt
- A0A162QQD4
- Pockets
- 20 · best druggability 0.88
Structure
electron microscopy · 1 distinct chain · 62% helix, 3% 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, b, c, d, e, f, g, h, i, j, k, l, m, n, o | Flagellin | protein | 302 | 62% helix, 3% strand | A0A162QQD4 |
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 | 962 | 0.88 | 0.90 | 133 | empty |
| 2 | 780 | 0.86 | 0.90 | 106 | empty |
| 3 | 700 | 0.86 | 0.90 | 93 | empty |
| 4 | 732 | 0.86 | 0.90 | 92 | empty |
| 5 | 666 | 0.86 | 0.90 | 90 | empty |
Interfaces
126 interfaces between chains.
- c–m · 2023 Ų buried · 20 hydrogen bonds · protein-protein
- C–H · 2020 Ų buried · 20 hydrogen bonds · protein-protein
- S–c · 2020 Ų buried · 20 hydrogen bonds · protein-protein
- J–T · 2019 Ų buried · 20 hydrogen bonds · protein-protein
- Z–j · 2019 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 5WJT · Cryo-EM structure of B. subtilis flagellar filaments N226Y · 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 A0A162QQD4
- Elsewhere: RCSB PDB 5WJT · PDBe 5WJT · UniProt A0A162QQD4
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