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Structural investigation of the TasA anchoring protein TapA from Bacillus subtilis
Analyse Structural investigation of the TasA anchoring protein TapA from Bacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HQC
- Type
- protein
- Length
- 116 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.28
- Source
- Bacillus subtilis
- Molecule
- TasA anchoring/assembly protein
- UniProt
- P40949
Structure
x-ray diffraction · resolution 1.28 · 1 distinct chain · 0% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TasA anchoring/assembly protein | protein | 116 | 0% helix, 47% strand | P40949 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6HQC · Structural investigation of the tasa anchoring protein tapa from bacillus subtilis · the same entry in another collection · chain A against A, TM-score 1.00
- P40949 · AlphaFold monomer V2.0 prediction for tasa ANCHORING/ASSEMBLY protein (P40949) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P40949
- Elsewhere: RCSB PDB 6HQC · PDBe 6HQC · UniProt P40949
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