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Structure of the catalytic subunit of telomerase, tert

Analyse Structure of the catalytic subunit of telomerase, tert in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3DU6
Type
protein
Length
1,192 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Telomerase reverse transcriptase
UniProt
Q0QHL8
Pockets
20 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BTelomerase reverse transcriptaseprotein59648% helix, 13% strandQ0QHL8

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16290.760.8262empty
22180.660.8435empty
32140.660.8436empty
4700.640.9218empty
5870.620.8817empty

Interfaces

1 interface between chains.

  • A–B · 876 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 3DU6 · Structure of the catalytic subunit of telomerase, TERT · the same entry in another collection · chain A against A, TM-score 1.00

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