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Crystal structure of bacillus thuringiensis CRY51AA1 protoxin at 1.65 ångströms resolution
Analyse Crystal structure of bacillus thuringiensis CRY51AA1 protoxin at 1.65 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PKM
- Type
- protein
- Length
- 305 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CRY51AA1
- UniProt
- A7IZR5
- Ligands
- GLY, SO4
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CRY51AA1 | protein | 305 | 11% helix, 58% strand | A7IZR5 |
Ligands and binding sites
- GLY · Glycine · ligand · 3 copies · chains A
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 79 | 0.48 | 0.83 | 17 | empty |
Compared structures
- 4PKM · Crystal Structure of Bacillus thuringiensis Cry51Aa1 Protoxin at 1.65 Angstroms Resolution · the same entry in another collection · 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 A7IZR5
- Elsewhere: RCSB PDB 4PKM · PDBe 4PKM · UniProt A7IZR5
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