› 5dsu

X-ray diffraction
1.93Å resolution

Crystal structure of double mutant of N-domain of human calmodulin

Released:
DOI: 10.2210/pdb5dsu/pdb
PDB entry 5dsu coloured by chain, front view.
PDB entry 5dsu coloured by chain, side view.
PDB entry 5dsu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
On the Ca2+ binding and conformational change in EF-hand domains: Experimental evidence of Ca2+-saturated intermediates of N-domain of calmodulin.
Ababou A, Zaleska M, Pfuhl M
Biochim Biophys Acta Proteins Proteom 1865 640-651 (2017)
PMID: 28288938

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143908 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calmodulin-1 Chain: A
Molecule details ›
Chain: A
Length: 78 amino acids
Theoretical weight: 8.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DP23 (Residues: 3-78; Coverage: 51%)
Gene names: CALM, CALM1, CAM, CAM1
Sequence domains: EF-hand domain pair

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P3221
Unit cell:
a: 38.4Å b: 38.4Å c: 81.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.23 0.228 0.264
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Domain-Based Protein Docking with Extremely Large Conformational Changes.
Christoffer et al. (2022)
1 more