Structure analysis

The crystal structure of the dimeric human importin alpha 1 at 2.5 angstrom resolution.

X-ray diffraction
2.528Å 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: 19031.07 Å2
Buried surface area: 2067.88 Å2
Dissociation area: 92.55 Å2
Dissociation energy (ΔGdiss): -1.77 kcal/mol
Dissociation entropy (TΔSdiss): 1.14 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-156490
Assembly 2 (preferred)
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Multimeric state: monomeric
Accessible surface area: 18951.33 Å2
Buried surface area: 1413.42 Å2
Dissociation area: 57.96 Å2
Dissociation energy (ΔGdiss): -0.89 kcal/mol
Dissociation entropy (TΔSdiss): 1.13 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-156490

Macromolecules

Chains: A, B
Length: 485 amino acids
Theoretical weight: 52.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P52292 (Residues: 70-529; Coverage: 87%)
Gene names: KPNA2, RCH1, SRP1
Pfam:
InterPro:
CATH: Leucine-rich Repeat Variant

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