Research workbench
Crystal structure of the trbd domain of tert and the CR4/5 of tr
Analyse Crystal structure of the trbd domain of tert and the CR4/5 of tr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4O26
- Type
- protein + RNA
- Length
- 562 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Telomerase reverse transcriptase; Telomerase tr
- UniProt
- Q1PS67
- Ligands
- SO4
- Pockets
- 13 · best druggability 0.73
Structure
x-ray diffraction · 3 distinct chains · 55% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Telomerase reverse transcriptase | protein | 240 | 56% helix, 5% strand | Q1PS67 |
| B | Telomerase reverse transcriptase | protein | 228 | 54% helix, 4% strand | Q1PS67 |
| E, F | Telomerase tr | rna | 47 | — | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 12 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1018 | 0.73 | 0.76 | 84 | SO4 |
| 2 | 486 | 0.63 | 0.77 | 34 | empty |
| 3 | 281 | 0.58 | 0.78 | 30 | SO4 |
| 4 | 308 | 0.57 | 0.76 | 39 | empty |
| 5 | 322 | 0.55 | 0.75 | 27 | empty |
Interfaces
4 interfaces between chains.
- A–E · 1342 Ų buried · 25 hydrogen bonds · protein-nucleic
- B–F · 1026 Ų buried · 14 hydrogen bonds · protein-nucleic
- A–B · 537 Ų buried · 12 hydrogen bonds · protein-protein
- B–E · 37 Ų buried · 1 hydrogen bond · protein-nucleic
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4O26 · Crystal structure of the TRBD domain of TERT and the CR4/5 of TR · the same entry in another collection · chain A against A, TM-score 1.00
- Q1PS67 · AlphaFold monomer V2.0 prediction for telomerase reverse transcriptase (Q1PS67) · a predicted model of the same protein · chain B against A, TM-score 0.92
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 Q1PS67
- Elsewhere: RCSB PDB 4O26 · PDBe 4O26 · UniProt Q1PS67
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