› 3w3z

X-ray diffraction
2.7Å resolution

Crystal structure of Kap121p bound to RanGTP

Released:
DOI: 10.2210/pdb3w3z/pdb
PDB entry 3w3z coloured by chain, front view.
PDB entry 3w3z coloured by chain, side view.
PDB entry 3w3z coloured by chain, top view.
Source organisms:
Primary publication:
Structural basis for cell-cycle-dependent nuclear import mediated by the karyopherin Kap121p.
Kobayashi J, Matsuura Y
J Mol Biol 425 1852-1868 (2013)
PMID: 23541588

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-542679 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Importin subunit beta-3 Chain: A
Molecule details ›
Chain: A
Length: 1089 amino acids
Theoretical weight: 122.3 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P32337 (Residues: 1-1089; Coverage: 100%)
Gene names: KAP121, PSE1, YM9952.10C, YMR308C
Sequence domains:
GTP-binding nuclear protein Ran Chain: B
Molecule details ›
Chain: B
Length: 176 amino acids
Theoretical weight: 20.21 KDa
Source organism: Canis lupus familiaris
Expression system: Escherichia coli
UniProt:
  • Canonical: P62825 (Residues: 1-176; Coverage: 82%)
Gene name: RAN
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand GTP 1 x GTP
1 modified residue:
Ligand MSE 25 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P3221
Unit cell:
a: 97.75Å b: 97.75Å c: 289.981Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.262 0.261 0.298
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The Structure of the Nuclear Pore Complex (An Update).
Lin et al. (2019)
5 more

4 mentions without citation

Karyopherin-mediated nucleocytoplasmic transport.
Wing et al. (2022)
3 more