Research workbench

Caspase 3 V266N

Analyse Caspase 3 V266N in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5IAN
Type: protein
Length: 247 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Caspase-3; Leu-ser-ser; ACE-asp-glu-val-ask
EC: 3.4.22.56
UniProt: P42574
Ligands: ACE, NA, 0QE

Structure

x-ray diffraction · 3 distinct chains · 28% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Caspase-3 (EC 3.4.22.56)	protein	240	29% helix, 26% strand	P42574
E	Leu-ser-ser	protein	3	0% helix, 0% strand	—
B	ACE-asp-glu-val-ask	protein	4	0% helix, 50% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · chains A, B
NA · Sodium ion · metal · chains A
0QE · Chloromethane · ion · chains A, B

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

Interfaces

2 interfaces between chains.

A–B · 481 Å² buried · 15 hydrogen bonds · protein-protein
A–E · 203 Å² buried · 1 hydrogen bond · protein-protein

Modifications

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

Compared structures

5IAN · Caspase 3 V266N · 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 0.98

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 5IAN · PDBe 5IAN · UniProt P42574

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