PDBe 1uhi

X-ray diffraction
1.8Å resolution

Crystal structure of i-aequorin

Released:
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
Macromolecule:
Aequorin-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 191 amino acids
Theoretical weight: 21.66 KDa
Source organism: Aequorea victoria
Expression system: Escherichia coli
UniProt:
  • Canonical: P02592 (Residues: 9-196; Coverage: 96%)
Sequence domains: EF hand
Structure domains: EF-hand

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P1
Unit cell:
a: 34.263Å b: 54.432Å c: 57.523Å
α: 102.05° β: 99.7° γ: 103.8°
R-values:
R R work R free
0.191 0.188 0.25
Expression system: Escherichia coli