› 4zj7

X-ray diffraction
2.4Å resolution

Crystal structure of the karyopherin Kap121p bound to the extreme C-terminus of the protein phosphatase Cdc14p

Released:
DOI: 10.2210/pdb4zj7/pdb
PDB entry 4zj7 coloured by chain, front view.
PDB entry 4zj7 coloured by chain, side view.
PDB entry 4zj7 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Crystal structure of the karyopherin Kap121p bound to the extreme C-terminus of the protein phosphatase Cdc14p.
Kobayashi J, Hirano H, Matsuura Y
Biochem Biophys Res Commun 463 309-14 (2015)
PMID: 26022122

Function and Biology Details

Reaction catalysed: 
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152268 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Importin subunit beta-3 Chain: A
Molecule details ›
Chain: A
Length: 1078 amino acids
Theoretical weight: 119.91 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P32337 (Residues: 1-1089; Coverage: 99%)
Gene names: KAP121, PSE1, YM9952.10C, YMR308C
Sequence domains:
Structure domains: Helix Hairpins
Tyrosine-protein phosphatase CDC14 Chain: B
Molecule details ›
Chain: B
Length: 35 amino acids
Theoretical weight: 3.83 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: Q00684 (Residues: 517-551; Coverage: 6%)
Gene names: CDC14, OAF3, YFR028C

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 77.263Å b: 127.758Å c: 131.789Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.219 0.252
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Karyopherin-mediated nucleocytoplasmic transport.
Wing et al. (2022)
5 other articles