Research workbench
Crystal structure of RAP1 and TRF2 complex
Analyse Crystal structure of RAP1 and TRF2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3K6G
- Type
- protein
- Length
- 380 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Telomeric repeat-binding factor 2-interacting protein 1; Telomeric repeat-binding factor 2
- UniProt
- Q9NYB0, Q15554
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 5 distinct chains · 69% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Telomeric repeat-binding factor 2-interacting protein 1 | protein | 93 | 71% helix, 0% strand | Q9NYB0 |
| B | Telomeric repeat-binding factor 2-interacting protein 1 | protein | 92 | 74% helix, 1% strand | Q9NYB0 |
| D | Telomeric repeat-binding factor 2 | protein | 33 | 67% helix, 0% strand | Q15554 |
| E | Telomeric repeat-binding factor 2 | protein | 36 | 58% helix, 3% strand | Q15554 |
| F | Telomeric repeat-binding factor 2 | protein | 33 | 64% helix, 3% strand | Q15554 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 485 | 0.65 | 0.77 | 44 | empty |
| 2 | 233 | 0.56 | 0.78 | 24 | empty |
| 3 | 210 | 0.53 | 0.78 | 27 | empty |
Interfaces
10 interfaces between chains.
- B–E · 1193 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 1109 Ų buried · 9 hydrogen bonds · protein-protein
- C–F · 1088 Ų buried · 10 hydrogen bonds · protein-protein
- A–E · 184 Ų buried · 3 hydrogen bonds · protein-protein
- E–F · 155 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 modified (engineered).
Compared structures
- 3K6G · Crystal structure of Rap1 and TRF2 complex · the same entry in another collection · chain F against F, TM-score 1.00
- Q9NYB0 · AlphaFold monomer V2.0 prediction for telomeric repeat-binding factor 2-interacting… · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q15554 · AlphaFold monomer V2.0 prediction for telomeric repeat-binding factor 2 (Q15554) · a predicted model of the same protein · chain F against A, TM-score 0.86
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 Q9NYB0
- Every structure of UniProt Q15554
- Elsewhere: RCSB PDB 3K6G · PDBe 3K6G · UniProt Q9NYB0 · UniProt Q15554
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