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Caspase-3 mutant- T152D

Analyse Caspase-3 mutant- T152D in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6BG4
Type
protein
Length
475 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
P42574
Ligands
ACE, 0QE, NA, CL, AZI

Structure

x-ray diffraction · 4 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B—protein141—P42574
E—protein92—P42574
F—protein93—P42574
C, D—protein4——

Ligands and binding sites

  • ACE · Acetyl group · ligand · 2 copies · chains E, C, F, D
  • 0QE · Chloromethane · ligand · 2 copies · chains A, E, C, B, F, D
  • NA · Sodium ion · metal · 13 copies · chains A, E, B, F
  • CL · Chloride ion · ion · 2 copies · chains A, B
  • AZI · Azide ion · ion · chains A, E

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

Compared structures

  • 6BG4 · Caspase-3 Mutant- T152D · the same entry in another collection · chain D against D, TM-score 1.00
  • P42574 · AlphaFold monomer V2.0 prediction for caspase-3 (P42574) · a predicted model of the same protein · chain B against A, TM-score 1.00

Analyse

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