› 3if7

X-ray diffraction
1.6Å resolution

Structure of Calmodulin complexed with its first endogenous inhibitor, sphingosylphosphorylcholine

Released:
DOI: 10.2210/pdb3if7/pdb
PDB 3if7 coloured by chain and viewed from the front.
PDB 3if7 coloured by chain and viewed from the side.
PDB 3if7 coloured by chain and viewed from the top.
Source organism: Bos taurus
Primary publication:
Structure and mechanism of calmodulin binding to a signaling sphingolipid reveal new aspects of lipid-protein interactions.
Kovacs E, Harmat V, Tóth J, Vértessy BG, Módos K, Kardos J, Liliom K
FASEB J. 24 3829-39 (2010)
PMID: 20522785

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calmodulin Chain: A
Molecule details ›
Chain: A
Length: 148 amino acids
Theoretical weight: 16.72 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P62157 (Residues: 2-149; Coverage: 99%)
Gene names: CALM, CAM
Sequence domains: EF-hand domain pair
Structure domains: EF-hand

Ligands and Environments

2 bound ligands:
Ligand CA 4 x CA
Ligand SPU 4 x SPU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P3221
Unit cell:
a: 39.669Å b: 39.669Å c: 170.34Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.192 0.238

Quick links

Citations

2 review citations

Emerging roles of sphingosylphosphorylcholine in modulating cardiovascular functions and diseases.
Ge et al. (2018)
1 more

2 mentions without citation

Structure and mechanism of calmodulin binding to a signaling sphingolipid reveal new aspects of lipid-protein interactions.
Kovacs et al. (2010)
1 more