Research workbench
Crystal structure of TRF1 and TERB1
Analyse Crystal structure of TRF1 and TERB1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XUP
- Type
- protein
- Length
- 416 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Telomeric repeat-binding factor 1; Telomere repeats-binding bouquet formation protein 1
- UniProt
- P54274, Q8NA31
- Pockets
- 5 · best druggability 0.58
Structure
x-ray diffraction · 4 distinct chains · 69% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Telomeric repeat-binding factor 1 | protein | 202 | 71% helix, 1% strand | P54274 |
| B | Telomeric repeat-binding factor 1 | protein | 196 | 74% helix, 0% strand | P54274 |
| C | Telomere repeats-binding bouquet formation protein 1 | protein | 12 | 0% helix, 17% strand | Q8NA31 |
| D | Telomere repeats-binding bouquet formation protein 1 | protein | 6 | 0% helix, 0% strand | Q8NA31 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 155 | 0.58 | 0.83 | 24 | empty |
| 2 | 126 | 0.57 | 0.83 | 20 | empty |
| 3 | 81 | 0.39 | 0.78 | 19 | empty |
| 4 | 95 | 0.36 | 0.75 | 19 | empty |
| 5 | 85 | 0.35 | 0.75 | 23 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1198 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 744 Ų buried · 18 hydrogen bonds · protein-protein
- B–D · 526 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 5XUP · Crystal structure of TRF1 and TERB1 · the same entry in another collection · chain D against D, TM-score 1.00
- P54274 · AlphaFold monomer V2.0 prediction for telomeric repeat-binding factor 1 (P54274) · a predicted model of the same protein · chain A against A, TM-score 0.98
- Q8NA31 · AlphaFold monomer V2.0 prediction for telomere repeats-binding bouquet formation protein… · a predicted model of the same protein · chain D against A, TM-score 0.43
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 P54274
- Every structure of UniProt Q8NA31
- Elsewhere: RCSB PDB 5XUP · PDBe 5XUP · UniProt P54274 · UniProt Q8NA31
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