› 1ziv

X-ray diffraction
2.31Å resolution

Catalytic Domain of Human Calpain-9

Released:
DOI: 10.2210/pdb1ziv/pdb
PDB entry 1ziv coloured by chain, front view.
PDB entry 1ziv coloured by chain, side view.
PDB entry 1ziv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structures of human calpains 1 and 9 imply diverse mechanisms of action and auto-inhibition.
Davis TL, Walker JR, Finerty PJ, Mackenzie F, Newman EM, Dhe-Paganon S
J Mol Biol 366 216-29 (2007)
PMID: 17157313

Function and Biology Details

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-127158 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calpain-9 Chain: A
Molecule details ›
Chain: A
Length: 339 amino acids
Theoretical weight: 38.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O14815 (Residues: 28-347; Coverage: 46%)
Gene names: CAPN9, NCL4
Sequence domains: Calpain family cysteine protease
Structure domains: Cysteine proteinases

Ligands and Environments

2 bound ligands:
Ligand CA 2 x CA
Ligand BME 2 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P2221
Unit cell:
a: 45.308Å b: 80.9Å c: 100.545Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.203 0.272
Expression system: Escherichia coli BL21

Quick links

Citations

6 review citations

Calpain research for drug discovery: challenges and potential.
Ono et al. (2016)
5 more

5 mentions without citation

Structural modeling of a novel CAPN5 mutation that causes uveitis and neovascular retinal detachment.
Bassuk et al. (2015)
4 more