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Conformational restrictions in the active site of unliganded human caspase-3

Analyse Conformational restrictions in the active site of unliganded human caspase-3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QX3
Type: protein
Length: 232 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Apopain
EC: 3.4.22.-
UniProt: P42574

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Apopain (EC 3.4.22.-)	protein	232	28% helix, 25% strand	P42574

Compared structures

1QX3 · Conformational restrictions in the active site of unliganded human 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 0.99

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 1QX3 · PDBe 1QX3 · UniProt P42574

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