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The role of loop bundle hydrogen bonds in the maturation and activity of (PRO)CASPASE-3

Analyse The role of loop bundle hydrogen bonds in the maturation and activity of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2J30
Type
protein
Length
249 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Caspase-3; ACE-asp-glu-val-asp-chloromethylketone inhibitor
EC
3.4.22.56
UniProt
P42574
Ligands
ACE, 0QE

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACaspase-3 (EC 3.4.22.56)protein24528% helix, 24% strandP42574
BACE-asp-glu-val-asp-chloromethylketone inhibitorprotein40% helix, 50% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · chains A, B
  • 0QE · Chloromethane · ion · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

  • A–B · 467 Ų buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

  • 2J30 · The Role of Loop Bundle Hydrogen Bonds in the Maturation and Activity of (Pro)caspase-3 · the same entry in another collection · chain A against A, TM-score 1.00
  • P42574 · AlphaFold monomer V2.0 prediction for caspase-3 (P42574) · a predicted model of the same protein · chain A against A, TM-score 0.96

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