Research workbench
Atxa protein, a virulence regulator from bacillus anthracis.
Analyse Atxa protein, a virulence regulator from bacillus anthracis. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4R6I
- Type
- protein
- Length
- 920 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anthrax toxin expression trans-acting positive regulator
- UniProt
- Q44636
- Pockets
- 12 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 60% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Anthrax toxin expression trans-acting positive regulator | protein | 472 | 60% helix, 7% strand | Q44636 |
| B | Anthrax toxin expression trans-acting positive regulator | protein | 448 | 61% helix, 6% strand | Q44636 |
Ligands and binding sites
- LMT · Dodecyl-beta-D-maltoside · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 842 | 0.80 | 0.82 | 75 | LMT |
| 2 | 184 | 0.80 | 0.94 | 33 | empty |
| 3 | 398 | 0.79 | 0.87 | 59 | empty |
| 4 | 393 | 0.78 | 0.87 | 45 | empty |
| 5 | 306 | 0.74 | 0.86 | 41 | empty |
Interfaces
1 interface between chains.
- A–B · 1520 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (engineered).
Compared structures
- 4R6I · AtxA protein, a virulence regulator from Bacillus anthracis. · the same entry in another collection · chain A against A, TM-score 1.00
- Q44636 · AlphaFold monomer V2.0 prediction for anthrax toxin expression trans- acting positive… · a predicted model of the same protein · chain B against A, TM-score 0.63
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 Q44636
- Elsewhere: RCSB PDB 4R6I · PDBe 4R6I · UniProt Q44636
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