› 3ekh

X-ray diffraction
2Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
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: 449 amino acids
Theoretical weight: 50.76 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P11799 (Residues: 1730-1763; Coverage: 2%)
  • Canonical: P42212 (Residues: 2-144, 191-192; Coverage: 61%)
  • Canonical: P0DP29 (Residues: 3-42, 45-149; Coverage: 97%)
Gene names: CaMI, Calm, Calm1, Cam, Cam1, GFP, Mylk
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GOL 1 x GOL
Ligand CA 4 x CA
1 modified residue:
Ligand CRO 1 x CRO

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P41212
Unit cell:
a: 121.648Å b: 121.648Å c: 97.327Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.224
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

44 review citations

The Growing and Glowing Toolbox of Fluorescent and Photoactive Proteins.
Rodriguez et al. (2017)
43 more

3 mentions without citation

Crystal structures of the GCaMP calcium sensor reveal the mechanism of fluorescence signal change and aid rational design.
Akerboom et al. (2009)
2 more