PDBe 1yr5

X-ray diffraction
1.7Å resolution

1.7-A structure of calmodulin bound to a peptide from DAP kinase

Released:
Source organism: Homo sapiens
Entry authors: Kursula P, Vahokoski J, Wilmanns M

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein. 

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Calmodulin-2 Chain: A
Molecule details ›
Chain: A
Length: 148 amino acids
Theoretical weight: 16.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DP24 (Residues: 2-149; Coverage: 99%)
Gene names: CALM2, CAM2, CAMB
Structure domains: EF-hand
Death-associated protein kinase 1 Chain: B
Molecule details ›
Chain: B
Length: 19 amino acids
Theoretical weight: 2.39 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P53355 (Residues: 302-320; Coverage: 1%)
Gene names: DAPK, DAPK1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: C2
Unit cell:
a: 66.07Å b: 33.71Å c: 75.89Å
α: 90° β: 111.16° γ: 90°
R-values:
R R work R free
0.203 0.2 0.257
Expression systems:
  • Escherichia coli
  • Not provided