› 5j3v

X-ray diffraction
3.05Å resolution

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

Released:
DOI: 10.2210/pdb5j3v/pdb
PDB entry 5j3v coloured by chain, front view.
PDB entry 5j3v coloured by chain, side view.
PDB entry 5j3v coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Karyopherin-β2 Recognition of a PY-NLS Variant that Lacks the Proline-Tyrosine Motif.
Soniat M, Chook YM
Structure 24 1802-1809 (2016)
PMID: 27618664

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159434 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transportin-1 Chains: A, B
Molecule details ›
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
Sequence domains:
Structure domains: Leucine-rich Repeat Variant
Histone H3.1 Chains: C, D
Molecule details ›
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

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2221
Unit cell:
a: 150.296Å b: 154.185Å c: 192.661Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.213 0.256
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Therapeutic Dissolution of Aberrant Phases by Nuclear-Import Receptors.
Guo et al. (2019)
3 more

4 mentions without citation

Nuclear import of histones.
Bernardes et al. (2020)
3 more