› 8hkw

X-ray diffraction
1.9Å resolution

Crystal structure of importin-alpha3 bound to the 53BP1 nuclear localization signal

Released:
DOI: 10.2210/pdb8hkw/pdb
Model geometry
Fit model/data
PDB entry 8hkw coloured by chain, front view.
PDB entry 8hkw coloured by chain, side view.
PDB entry 8hkw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystallographic data of an importin-α3 dimer in which the two protomers are bridged by a bipartite nuclear localization signal.
Matsuura Y
OpenAccess logo Data Brief 47 108988 (2023)
PMID: 36875212

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-271484 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Importin subunit alpha-3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 416 amino acids
Theoretical weight: 45.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00629 (Residues: 70-485; Coverage: 80%)
Gene names: KPNA4, QIP1
Sequence domains:
TP53-binding protein 1 Chains: C, D
Molecule details ›
Chains: C, D
Length: 22 amino acids
Theoretical weight: 2.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12888 (Residues: 1665-1686; Coverage: 1%)
Gene name: TP53BP1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Unit cell:
a: 95.703Å b: 79.6Å c: 117.44Å
α: 90° β: 95.57° γ: 90°
R-values:
R R work R free
0.202 0.201 0.221
Expression system: Escherichia coli

Quick links

Citations

1 mention without citation

Crystallographic data of an importin-α3 dimer in which the two protomers are bridged by a bipartite nuclear localization signal.
Matsuura Y. (2023)