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Crystal structure of caspase 3 S150A

Analyse Crystal structure of caspase 3 S150A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6BDV
Type
protein
Length
238 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Caspase-3 subunit P17; Caspase-3 subunit P12; Acetyl-asp-glu-val-asp-cmk
EC
3.4.22.56
UniProt
P42574
Ligands
ACE, AZI, 0QE, CL

Structure

x-ray diffraction · 3 distinct chains · 29% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACaspase-3 subunit P17 (EC 3.4.22.56)protein14127% helix, 30% strandP42574
BCaspase-3 subunit P12 (EC 3.4.22.56)protein9333% helix, 18% strandP42574
CAcetyl-asp-glu-val-asp-cmkprotein40% helix, 50% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · chains B, C
  • AZI · Azide ion · ion · 2 copies · chains A, B
  • 0QE · Chloromethane · ion · chains A, B, C
  • CL · Chloride ion · ion · chains A

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

Interfaces

3 interfaces between chains.

  • A–B · 2165 Ų buried · 33 hydrogen bonds · protein-protein
  • B–C · 398 Ų buried · 11 hydrogen bonds · protein-protein
  • A–C · 199 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 6BDV · Crystal structure of Caspase 3 S150A · 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 1.00

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