Research workbench
Structure of tribolium telomerase in complex with the highly specific inhibitor BIBR1532
Analyse Structure of tribolium telomerase in complex with the highly specific inhibitor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CQG
- 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
- Ligands
- 55C
- Pockets
- 20 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Telomerase reverse transcriptase | protein | 596 | 48% helix, 13% strand | Q0QHL8 |
Ligands and binding sites
- 55C · 2-{[(2E)-3-(naphthalen-2-yl)but-2-enoyl]amino}benzoic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 311 | 0.73 | 0.86 | 32 | empty |
| 2 | 257 | 0.68 | 0.84 | 36 | empty |
| 3 | 83 | 0.66 | 0.92 | 21 | empty |
| 4 | 226 | 0.66 | 0.84 | 37 | empty |
| 5 | 325 | 0.61 | 0.78 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 890 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 5CQG · Structure of Tribolium telomerase in complex with the highly specific inhibitor BIBR1532 · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q0QHL8
- Elsewhere: RCSB PDB 5CQG · PDBe 5CQG · UniProt Q0QHL8
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