› 1xe0

X-ray diffraction
1.7Å resolution

The structure and function of Xenopus NO38-core, a histone binding chaperone in the nucleolus

Released:
DOI: 10.2210/pdb1xe0/pdb
PDB entry 1xe0 coloured by chain, front view.
PDB entry 1xe0 coloured by chain, side view.
PDB entry 1xe0 coloured by chain, top view.
Source organism: Xenopus laevis
Primary publication:
The structure and function of Xenopus NO38-core, a histone chaperone in the nucleolus.
Namboodiri VM, Akey IV, Schmidt-Zachmann MS, Head JF, Akey CW
Structure 12 2149-60 (2004)
PMID: 15576029

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139437 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nucleophosmin Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 114 amino acids
Theoretical weight: 12.35 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07222 (Residues: 16-124; Coverage: 37%)
Gene name: npm1
Sequence domains: Nucleoplasmin/nucleophosmin domain
Structure domains: Nucleoplasmin core domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P1
Unit cell:
a: 59Å b: 59Å c: 87.2Å
α: 77° β: 88.3° γ: 60.9°
R-values:
R R work R free
0.212 0.208 0.259
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

19 review citations

Nucleophosmin and cancer.
Grisendi et al. (2006)
18 more

3 mentions without citation

Structure-function relationship of H2A-H2B specific plant histone chaperones.
Kumar et al. (2020)
2 more