1UFI: Dimerization domain of human CENP-B

Crystal structure of the dimerization domain of human CENP-B. Determined by X-ray diffraction at 1.65 Å resolution. Released 17 Feb 2004.

Method
X-ray diffraction
Resolution
1.65 Å
Organism
Homo sapiens
Chains
4
Atoms
1,694
Mol. weight
29 kDa
Released
17 Feb 2004

Explore 1UFI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1UFI contains 11 α-helices and 0 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix9-2315
α-helix30-4920
Chain B: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix6-83
α-helix9-2416
α-helix30-4920
Chain C: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix4-85
α-helix9-2315
α-helix30-4819
Chain D: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix5-84
α-helix9-2416
α-helix30-4718

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Major centromere autoantigen BA, B, C, Dprotein64Homo sapiensP07199 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>1UFI_1 Major centromere autoantigen B (chains A, B, C, D)
GSHMPVPSFGEAMAYFAMVKRYLTSFPIDDRVQSHILHLEHDLVHVTRKNHARQAGVRGL
GHQS

Primary citation

Crystal structure of the human centromere protein B (CENP-B) dimerization domain at 1.65-A resolution. Tawaramoto, M.S., Park, S.-Y., Tanaka, Y. et al. J Biol Chem (2003) 278:51454-51461. DOI 10.1074/jbc.M310388200 · PubMed

Other PDB entries of the same protein (UniProt P07199 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 1UFI directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.