› 1ufi

X-ray diffraction
1.65Å resolution

Crystal structure of the dimerization domain of human CENP-B

Released:
DOI: 10.2210/pdb1ufi/pdb
PDB entry 1ufi coloured by chain, front view.
PDB entry 1ufi coloured by chain, side view.
PDB entry 1ufi coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the human centromere protein B (CENP-B) dimerization domain at 1.65-A resolution.
Tawaramoto MS, Park SY, Tanaka Y, Nureki O, Kurumizaka H, Yokoyama S
J Biol Chem 278 51454-61 (2003)
PMID: 14522975

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-139426 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major centromere autoantigen B Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 64 amino acids
Theoretical weight: 7.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07199 (Residues: 540-599; Coverage: 10%)
Gene name: CENPB
Sequence domains: Centromere protein B dimerisation domain
Structure domains: Dimerisation domain of CENP-B

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P212121
Unit cell:
a: 43.707Å b: 48.955Å c: 100.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.232 0.309
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Diverse mechanisms of centromere specification.
Mellone et al. (2021)
2 more

2 mentions without citation

Pogo-like transposases have been repeatedly domesticated into CENP-B-related proteins.
Mateo et al. (2014)
1 more