Research workbench
Structure of telomerase from candida tropicalis in complexe with twj fragment of telomeric RNA
Analyse Structure of telomerase from candida tropicalis in complexe with twj fragment… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZDP
- Type
- protein + RNA
- Length
- 750 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Telomerase reverse transcriptase; Chains: B
- EC
- 2.7.7.49
- UniProt
- C5MCQ7
- Ligands
- K
- Pockets
- 16 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Telomerase reverse transcriptase (EC 2.7.7.49) | protein | 683 | 48% helix, 12% strand | C5MCQ7 |
| B | Chains: B | rna | 67 | — | — |
Ligands and binding sites
- K · Potassium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 736 | 0.78 | 0.82 | 81 | empty |
| 2 | 82 | 0.65 | 0.90 | 17 | empty |
| 3 | 176 | 0.63 | 0.84 | 24 | empty |
| 4 | 468 | 0.62 | 0.76 | 25 | empty |
| 5 | 111 | 0.60 | 0.87 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1362 Ų buried · 22 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 11 modified (engineered).
Compared structures
- 6ZDP · Structure of telomerase from Candida Tropicalis in complexe with TWJ fragment of… · 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 C5MCQ7
- Elsewhere: RCSB PDB 6ZDP · PDBe 6ZDP · UniProt C5MCQ7
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