› 5cqg

X-ray diffraction
2.3Å resolution

Structure of Tribolium telomerase in complex with the highly specific inhibitor BIBR1532

Released:
DOI: 10.2210/pdb5cqg/pdb
PDB entry 5cqg coloured by chain, front view.
PDB entry 5cqg coloured by chain, side view.
PDB entry 5cqg coloured by chain, top view.
Source organism: Tribolium castaneum
Primary publication:
Structural Basis of Telomerase Inhibition by the Highly Specific BIBR1532.
Bryan C, Rice C, Hoffman H, Harkisheimer M, Sweeney M, Skordalakes E
Structure 23 1934-1942 (2015)
PMID: 26365799

Function and Biology Details

Reaction catalysed: 
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-171089 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Telomerase reverse transcriptase Chains: A, B
Molecule details ›
Chains: A, B
Length: 596 amino acids
Theoretical weight: 70.59 KDa
Source organism: Tribolium castaneum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q0QHL8 (Residues: 1-596; Coverage: 100%)
Gene names: AUGUSTUS-3.0.2_10963, TERT, TcasGA2_TC010963
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 55C 2 x 55C
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 117.719Å b: 84.902Å c: 123.333Å
α: 90° β: 116.2° γ: 90°
R-values:
R R work R free
0.237 0.235 0.273
Expression system: Escherichia coli

Quick links

Citations

22 review citations

Roles of telomeres and telomerase in cancer, and advances in telomerase-targeted therapies.
Jafri et al. (2016)
21 more

10 mentions without citation

Structural biology of telomerase and its interaction at telomeres.
Wang et al. (2017)
9 more