X-ray diffraction
1.8Å resolution

Crystal structure of br-aequorin

Source organism: Aequorea victoria
Primary publication:
The crystal structures of semi-synthetic aequorins.
Protein Sci. 14 409-16 (2005)
PMID: 15632284

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Aequorin-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 191 amino acids
Theoretical weight: 21.89 KDa
Source organism: Aequorea victoria
Expression system: Escherichia coli
  • Canonical: P02592 (Residues: 9-196; Coverage: 96%)
Sequence domains: EF hand
Structure domains: EF-hand

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P1
Unit cell:
a: 34.213Å b: 56.983Å c: 57.82Å
α: 72.22° β: 80.32° γ: 68.01°
R R work R free
0.163 0.162 0.198
Expression system: Escherichia coli