X-ray diffraction
2Å resolution

Structure of the R75A mutant of rat alpha-Parvalbumin

Source organism: Rattus norvegicus
Primary publication:
Removing the invariant salt bridge of parvalbumin increases flexibility in the AB-loop structure.
Acta Crystallogr. D Biol. Crystallogr. 65 733-43 (2009)
PMID: 19622856

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Parvalbumin alpha Chain: A
Molecule details ›
Chain: A
Length: 109 amino acids
Theoretical weight: 11.73 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P02625 (Residues: 2-110; Coverage: 99%)
Gene names: Pva, Pvalb
Sequence domains: EF-hand domain pair
Structure domains: EF-hand

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 27.315Å b: 55.05Å c: 28.768Å
α: 90° β: 105.56° γ: 90°
R R work R free
0.158 0.144 0.205
Expression system: Escherichia coli BL21(DE3)