3evr

X-ray diffraction
2Å resolution

Crystal structure of Calcium bound monomeric GCAMP2

Released:
Primary publication:
Structural basis for calcium sensing by GCaMP2.
Structure 16 1817-27 (2008)
PMID: 19081058

Function and Biology Details

Reaction catalysed:
ATP + [myosin light-chain] = ADP + [myosin light-chain] phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-144017 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calmodulin-1; Green fluorescent protein; Myosin light chain kinase, smooth muscle, deglutamylated form Chain: A
Molecule details ›
Chain: A
Length: 411 amino acids
Theoretical weight: 46.41 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P11799 (Residues: 1730-1763; Coverage: 2%)
  • Canonical: P42212 (Residues: 2-144, 151-170, 191-192; Coverage: 69%)
  • Canonical: P0DP29 (Residues: 23-42, 45-148; Coverage: 83%)
Gene names: CaMI, Calm, Calm1, Cam, Cam1, GFP, Mylk
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P41212
Unit cell:
a: 121.995Å b: 121.995Å c: 97.831Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.163 0.19
Expression system: Escherichia coli