Research workbench
Structure of telomerase from candida albicans in complexe with twj fragment of telomeric RNA
Analyse Structure of telomerase from candida albicans in complexe with twj fragment of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZDU
- Type
- protein + RNA
- Length
- 1,516 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Telomerase reverse transcriptase; Chains: C,D
- EC
- 2.7.7.49
- UniProt
- A0A1D8PEA0
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Telomerase reverse transcriptase (EC 2.7.7.49) | protein | 693 | 49% helix, 11% strand | A0A1D8PEA0 |
| C, D | Chains: C,D | rna | 65 | — | — |
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 | 1056 | 0.79 | 0.81 | 67 | empty |
| 2 | 710 | 0.78 | 0.82 | 48 | empty |
| 3 | 471 | 0.75 | 0.83 | 59 | empty |
| 4 | 424 | 0.72 | 0.82 | 59 | empty |
| 5 | 420 | 0.67 | 0.79 | 48 | empty |
Interfaces
4 interfaces between chains.
- A–B · 2470 Ų buried · 31 hydrogen bonds · protein-protein
- A–C · 2006 Ų buried · 45 hydrogen bonds · protein-nucleic
- B–D · 1985 Ų buried · 42 hydrogen bonds · protein-nucleic
- C–D · 951 Ų buried · 41 hydrogen bonds · nucleic-nucleic
Compared structures
- 6ZDU · Structure of telomerase from Candida albicans in complexe with TWJ fragment of telomeric… · 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 A0A1D8PEA0
- Elsewhere: RCSB PDB 6ZDU · PDBe 6ZDU · UniProt A0A1D8PEA0
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