› 5vch

X-ray diffraction
2.35Å resolution

Crystal structure of full-length Kluyveromyces lactis Kap123

Released:
DOI: 10.2210/pdb5vch/pdb
PDB entry 5vch coloured by chain, front view.
PDB entry 5vch coloured by chain, side view.
PDB entry 5vch coloured by chain, top view.
Source organism: Kluyveromyces lactis
Primary publication:
Structure-based nuclear import mechanism of histones H3 and H4 mediated by Kap123.
An S, Yoon J, Kim H, Song JJ, Cho US
Elife 6 (2017)
PMID: 29035199

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179452 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Importin N-terminal domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 1116 amino acids
Theoretical weight: 123.53 KDa
Source organism: Kluyveromyces lactis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6CMF0 (Residues: 2-1113; Coverage: 100%)
Gene name: KLLA0_E20769g
Sequence domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 24 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P1
Unit cell:
a: 79.05Å b: 88.12Å c: 102.01Å
α: 79.19° β: 80.03° γ: 70.98°
R-values:
R R work R free
0.21 0.21 0.235
Expression system: Escherichia coli

Quick links

Citations

4 review citations

H3-H4 Histone Chaperone Pathways.
Grover et al. (2018)
3 more

1 mention without citation

Structure of IMPORTIN-4 bound to the H3-H4-ASF1 histone-histone chaperone complex.
Bernardes et al. (2022)