Research workbench
Crystal structure of the cytosolic domain of B. subtilis flha
Analyse Crystal structure of the cytosolic domain of B. subtilis flha in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MIX
- Type
- protein
- Length
- 313 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar biosynthesis protein flha
- UniProt
- P35620
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flagellar biosynthesis protein flha | protein | 313 | 53% helix, 13% strand | P35620 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 94 | 0.43 | 0.78 | 25 | empty |
| 2 | 62 | 0.34 | 0.77 | 16 | empty |
Compared structures
- 3MIX · Crystal structure of the cytosolic domain of B. subtilis FlhA · the same entry in another collection · chain A against A, TM-score 1.00
- P35620 · AlphaFold monomer V2.0 prediction for flagellar biosynthesis protein flha (P35620) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P35620
- Elsewhere: RCSB PDB 3MIX · PDBe 3MIX · UniProt P35620
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