2L3N: Rap1-Taz1 fusion protein

Solution structure of Rap1-Taz1 fusion protein. Determined by solution NMR. Released 12 Jan 2011.

Method: Solution NMR
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Chains: 1
Atoms: 777
Mol. weight: 11.12 kDa
Released: 12 Jan 2011

Explore 2L3N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2L3N contains 6 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: 6 helices, 0 β-strands

Element	Residues	Length
α-helix	3-5	3
α-helix	10-25	16
α-helix	29-39	11
α-helix	43-51	9
α-helix	61-63	3
α-helix	85-98	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DNA-binding protein rap1,Telomere length regulator taz1	A	protein	104	Schizosaccharomyces pombe (strain 972 / ATCC 24843)	P79005 (AlphaFold model), Q96TL7 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2L3N_1 DNA-binding protein rap1,Telomere length regulator taz1 (chains A)
SVSILRSSVNHREVDEAIDNILRYTNSTEQQFLEAMESTGGRVRIAIAKLLSKQTSGGSG
GSKLGGSGGSRKDLSVKGMLYDSDSQQILNRLRERVSGSTAQSA

Primary citation

A conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organisms. Chen, Y., Rai, R., Zhou, Z.R. et al. Nat Struct Mol Biol (2011) 18:213-221. DOI 10.1038/nsmb.1974 · PubMed

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

4ZMK 1.5 Å, Crystal structure of the dimerization domain of S. pombe Taz1
4ZMI 2.3 Å, Crystal structure of the Helical domain of S. pombe Taz1

Browse structure collections

About this viewer

MolViewer shows 2L3N 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.