Research workbench

Caspase-3 T140F

Analyse Caspase-3 T140F in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4QUD
Type: protein
Length: 476 residues
Chains: 4
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
Pockets: 3 · best druggability 0.65

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Caspase-3 (EC 3.4.22.56)	protein	238	29% helix, 25% strand	P42574
B	Caspase-3 (EC 3.4.22.56)	protein	230	30% helix, 27% strand	P42574
D, C	ACE-asp-glu-val-asp-chloromethylketone inhibitor	protein	4	0% helix, 50% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · 2 copies · chains A, D, B, C
0QE · Chloromethane · ion · 2 copies · chains A, D, B, C

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

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	290	0.65	0.81	35	empty
2	62	0.34	0.76	18	empty
3	53	0.32	0.78	15	empty

Interfaces

3 interfaces between chains.

A–B · 2218 Å² buried · 43 hydrogen bonds · protein-protein
B–C · 475 Å² buried · 20 hydrogen bonds · protein-protein
A–D · 470 Å² buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

4QUD · Caspase-3 T140F · 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 B against A, TM-score 0.99

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 P42574
Elsewhere: RCSB PDB 4QUD · PDBe 4QUD · UniProt P42574

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.