4ZMK: Dimerization domain of S. pombe Taz1

Crystal structure of the dimerization domain of S. pombe Taz1. Determined by X-ray diffraction at 1.5 Å resolution. Released 23 Sept 2015.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Chains: 1
Atoms: 639
Mol. weight: 7.61 kDa
Released: 23 Sept 2015

Explore 4ZMK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ZMK contains 3 α-helices and 0 β-strands across 1 chain. 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: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	410-414	5
α-helix	427-447	21
α-helix	451-477	27

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Telomere length regulator taz1	A	protein	71	Schizosaccharomyces pombe (strain 972 / ATCC 24843)	P79005 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4ZMK_1 Telomere length regulator taz1 (chains A)
DTFSERTLGLNSIDNTEISEVVSLGLVSSALDKITGLLSADNLSETVSQARDFSHTLSKS
LKSRAKSLSQK

Primary citation

Fission yeast telomere-binding protein Taz1 is a functional but not a structural counterpart of human TRF1 and TRF2. Deng, W., Wu, J., Wang, F. et al. Cell Res (2015) 25:881-884. DOI 10.1038/cr.2015.76 · PubMed

Other PDB entries of the same protein (UniProt P79005 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4ZMI 2.3 Å, Crystal structure of the Helical domain of S. pombe Taz1
2L3N Solution structure of Rap1-Taz1 fusion protein

Browse structure collections

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