Research workbench
Crystal structure of the ten domain of the telomerase reverse transcriptase
Analyse Crystal structure of the ten domain of the telomerase reverse transcriptase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2B2A
- Type
- protein
- Length
- 475 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Telomerase reverse transcriptase
- EC
- 2.7.7.49
- UniProt
- O77448
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 3 distinct chains · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Telomerase reverse transcriptase (EC 2.7.7.49) | protein | 164 | 43% helix, 20% strand | O77448 |
| B | Telomerase reverse transcriptase (EC 2.7.7.49) | protein | 154 | 44% helix, 21% strand | O77448 |
| C | Telomerase reverse transcriptase (EC 2.7.7.49) | protein | 157 | 43% helix, 19% strand | O77448 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 524 | 0.65 | 0.77 | 48 | empty |
| 2 | 239 | 0.60 | 0.80 | 40 | empty |
| 3 | 96 | 0.33 | 0.73 | 20 | empty |
| 4 | 52 | 0.24 | 0.72 | 14 | empty |
Interfaces
3 interfaces between chains.
- A–B · 779 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 618 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 332 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2B2A · Crystal Structure of the TEN domain of the Telomerase Reverse Transcriptase · the same entry in another collection · chain A against A, TM-score 1.00
- O77448 · AlphaFold monomer V2.0 prediction for telomerase reverse transcriptase (O77448) · a predicted model of the same protein · chain B against A, TM-score 0.35
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 O77448
- Elsewhere: RCSB PDB 2B2A · PDBe 2B2A · UniProt O77448
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