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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).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACRY51AA1protein30511% helix, 58% strandA7IZR5

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1790.480.8317empty

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

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