Structure analysis

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

X-ray diffraction
1.05Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: monomeric
Accessible surface area: 7122.52 Å2
Buried surface area: 355.69 Å2
Dissociation area: 64.8 Å2
Dissociation energy (ΔGdiss): -2.07 kcal/mol
Dissociation entropy (TΔSdiss): 1.52 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-192632
Assembly 2 (preferred)
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Multimeric state: monomeric
Accessible surface area: 7151.17 Å2
Buried surface area: 440.4 Å2
Dissociation area: 133.69 Å2
Dissociation energy (ΔGdiss): -3.71 kcal/mol
Dissociation entropy (TΔSdiss): 1.44 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-192632

Macromolecules

Chains: A, B
Length: 131 amino acids
Theoretical weight: 15.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9NVD7 (Residues: 242-372; Coverage: 35%)
Gene names: MXRA2, PARVA
Pfam: Calponin homology (CH) domain
InterPro:
CATH: Calponin-like domain

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