› 2l42

Solution NMR

The solution structure of Rap1 BRCT domain from Saccharomyces cerevisiae

Released:
DOI: 10.2210/pdb2l42/pdb
PDB entry 2l42 coloured by chain, ensemble of 20 models, front view.
PDB entry 2l42 coloured by chain, ensemble of 20 models, side view.
PDB entry 2l42 coloured by chain, ensemble of 20 models, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Solution structure of Rap1 BRCT domain from Saccharomyces cerevisiae reveals a novel fold.
Zhang W, Zhang J, Zhang X, Xu C, Tu X
Biochem Biophys Res Commun 404 1055-9 (2011)
PMID: 21187076

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145985 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA-binding protein RAP1 Chain: A
Molecule details ›
Chain: A
Length: 106 amino acids
Theoretical weight: 12.19 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P11938 (Residues: 116-212; Coverage: 12%)
Gene names: GRF1, N1310, RAP1, TUF1, YNL216W
Sequence domains: BRCT domain, a BRCA1 C-terminus domain
Structure domains: BRCT domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

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Citations

1 review citation

Telomerase and telomere-associated proteins: structural insights into mechanism and evolution.
Lewis et al. (2012)
5 other articles

5 mentions without citation

Structural and functional analyses of the mammalian TIN2-TPP1-TRF2 telomeric complex.
Hu et al. (2017)
4 more