Structure analysis

Crystal structure of human Karyopherin-beta2 bound to the histone H3 tail

X-ray diffraction
3.05Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 38446.56 Å2
Buried surface area: 1754.25 Å2
Dissociation area: 877.12 Å2
Dissociation energy (ΔGdiss): 0.16 kcal/mol
Dissociation entropy (TΔSdiss): 8.65 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-159434
Assembly 2
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Multimeric state: hetero dimer
Accessible surface area: 38582.95 Å2
Buried surface area: 1844.48 Å2
Dissociation area: 922.24 Å2
Dissociation energy (ΔGdiss): 4.47 kcal/mol
Dissociation entropy (TΔSdiss): 8.61 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-159434

Macromolecules

Chains: A, B
Length: 854 amino acids
Theoretical weight: 96.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92973 (Residues: 9-331, 375-898; Coverage: 94%)
Gene names: KPNB2, MIP1, TNPO1, TRN
Pfam:
InterPro:
CATH: Leucine-rich Repeat Variant

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Chains: C, D
Length: 17 amino acids
Theoretical weight: 1.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P68431 (Residues: 12-28; Coverage: 13%)
Gene names: H3C1, H3C10, H3C11, H3C12, H3C2, H3C3, H3C4, H3C6, H3C7, H3C8, H3FA, H3FB, H3FC HIST1H3C, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL, HIST1H3A, HIST1H3B, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J
InterPro: Histone H3/CENP-A

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