Research workbench
Lepidoptera-specific toxin CRY1AC from bacillus thuringiensis ssp. kurstaki hd-73
Analyse Lepidoptera-specific toxin CRY1AC from bacillus thuringiensis ssp. kurstaki… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ARX
- Type
- protein
- Length
- 2,309 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pesticidal crystal protein CRY1AC
- UniProt
- P05068
- Ligands
- 13D
- Pockets
- 19 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 36% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pesticidal crystal protein CRY1AC | protein | 578 | 36% helix, 28% strand | P05068 |
| B | Pesticidal crystal protein CRY1AC | protein | 578 | 36% helix, 29% strand | P05068 |
| C | Pesticidal crystal protein CRY1AC | protein | 577 | 36% helix, 28% strand | P05068 |
| D | Pesticidal crystal protein CRY1AC | protein | 576 | 37% helix, 28% strand | P05068 |
Ligands and binding sites
- 13D · 1,3-diaminopropane · ligand · 4 copies · chains A, D, B, C
- GOL · Glycerol · additive · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1055 | 0.78 | 0.80 | 97 | empty |
| 2 | 1017 | 0.74 | 0.77 | 101 | empty |
| 3 | 363 | 0.69 | 0.82 | 37 | empty |
| 4 | 336 | 0.68 | 0.82 | 36 | empty |
| 5 | 341 | 0.68 | 0.82 | 34 | empty |
Interfaces
5 interfaces between chains.
- B–C · 604 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 529 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 371 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 308 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 228 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4ARX · Lepidoptera-specific toxin Cry1Ac from Bacillus thuringiensis ssp. kurstaki HD-73 · the same entry in another collection · chain D against D, TM-score 1.00
- P05068 · AlphaFold monomer V2.0 prediction for pesticidal crystal protein CRY1AC (P05068) · a predicted model of the same protein · chain A against A, 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 P05068
- Elsewhere: RCSB PDB 4ARX · PDBe 4ARX · UniProt P05068
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.