Research workbench
Structure of the flagellar motab stator complex from bacillus subtilis
Analyse Structure of the flagellar motab stator complex from bacillus subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YSL
- Type
- protein
- Length
- 1,324 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Motility protein a; Motility protein B
- UniProt
- P28611, P28612
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 4 distinct chains · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| G, F | Motility protein a | protein | 254 | 65% helix, 0% strand | P28611 |
| A | Motility protein B | protein | 26 | 69% helix, 0% strand | P28612 |
| B | Motility protein B | protein | 25 | 72% helix, 0% strand | P28612 |
| E, D, C | Motility protein a | protein | 255 | 67% helix, 0% strand | P28611 |
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1087 | 0.82 | 0.83 | 110 | empty |
| 2 | 750 | 0.76 | 0.81 | 69 | empty |
| 3 | 79 | 0.74 | 0.96 | 16 | empty |
| 4 | 75 | 0.70 | 0.94 | 24 | empty |
| 5 | 317 | 0.69 | 0.83 | 39 | empty |
Interfaces
15 interfaces between chains.
- F–E · 2059 Ų buried · 9 hydrogen bonds · protein-protein
- G–C · 2042 Ų buried · 7 hydrogen bonds · protein-protein
- D–C · 2003 Ų buried · 15 hydrogen bonds · protein-protein
- G–F · 1804 Ų buried · 9 hydrogen bonds · protein-protein
- E–D · 1731 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6YSL · Structure of the flagellar MotAB stator complex from Bacillus subtilis · the same entry in another collection · chain C against C, TM-score 1.00
- P28611 · AlphaFold monomer V2.0 prediction for motility protein a (P28611) · a predicted model of the same protein · chain G against A, TM-score 0.95
- P28612 · AlphaFold monomer V2.0 prediction for motility protein B (P28612) · a predicted model of the same protein · chain B against A, TM-score 0.76
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 P28611
- Every structure of UniProt P28612
- Elsewhere: RCSB PDB 6YSL · PDBe 6YSL · UniProt P28611 · UniProt P28612
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