› 1sji

X-ray diffraction
2.4Å resolution

Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerization

Released:
DOI: 10.2210/pdb1sji/pdb
PDB entry 1sji coloured by chain, front view.
PDB entry 1sji coloured by chain, side view.
PDB entry 1sji coloured by chain, top view.
Source organism: Canis lupus familiaris
Primary publication:
Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerization.
Park H, Park IY, Kim E, Youn B, Fields K, Dunker AK, Kang C
J Biol Chem 279 18026-33 (2004)
PMID: 14871888

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146273 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calsequestrin-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 350 amino acids
Theoretical weight: 40.75 KDa
Source organism: Canis lupus familiaris
Expression system: Escherichia coli
UniProt:
  • Canonical: P12637 (Residues: 22-371; Coverage: 90%)
Gene name: CASQ2
Sequence domains: Calsequestrin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: I4
Unit cell:
a: 145.188Å b: 145.188Å c: 99.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.192 0.241
Expression system: Escherichia coli

Quick links

Citations

22 review citations

GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum.
Marzec et al. (2012)
21 more

9 mentions without citation

Protonation and pK changes in protein-ligand binding.
Onufriev et al. (2013)
8 more