› 1zcm

X-ray diffraction
2Å resolution

Human calpain protease core inhibited by ZLLYCH2F

Released:
DOI: 10.2210/pdb1zcm/pdb
PDB entry 1zcm coloured by chain, front view.
PDB entry 1zcm coloured by chain, side view.
PDB entry 1zcm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular mode of action of a covalently inhibiting peptidomimetic on the human calpain protease core.
Li Q, Hanzlik RP, Weaver RF, Schönbrunn E
Biochemistry 45 701-8 (2006)
PMID: 16411745

Function and Biology Details

Reaction catalysed: 
Broad endopeptidase specificity.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139576 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calpain-1 catalytic subunit Chain: A
Molecule details ›
Chain: A
Length: 321 amino acids
Theoretical weight: 36.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07384 (Residues: 33-353; Coverage: 45%)
Gene names: CANPL1, CAPN1, PIG30
Sequence domains: Calpain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

2 bound ligands:
Ligand CA 2 x CA
Ligand C1N 1 x C1N
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 50.44Å b: 62.74Å c: 99.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.182 0.223
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

The calpains: modular designs and functional diversity.
Croall et al. (2007)
3 more

13 mentions without citation

Immunomodulatory Action of Substituted 1,3,4-Thiadiazines on the Course of Myocardial Infarction.
Sarapultsev et al. (2018)
12 more