X-ray diffraction
1.05Å resolution

Crystal structure of the C-terminal calponin homology domain of alpha parvin


Function and Biology Details

Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Alpha-parvin Chains: A, B
Molecule details ›
Chains: A, B
Length: 131 amino acids
Theoretical weight: 15.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
  • Canonical: Q9NVD7 (Residues: 242-372; Coverage: 35%)
Gene names: MXRA2, PARVA
Sequence domains: Calponin homology (CH) domain
Structure domains: Calponin-like domain

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 44.144Å b: 71.197Å c: 47.146Å
α: 90° β: 99.88° γ: 90°
R R work R free
0.144 0.143 0.159
Expression system: Escherichia coli BL21