Research workbench
Crystal structure of ngtrf complexed with telomeric DNA
Analyse Crystal structure of ngtrf complexed with telomeric DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QHB
- Type
- protein + DNA
- Length
- 199 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-D(P*TP*TP*TP*AP*GP*GP*G)-3'; 5'-D(P*CP*CP*CP*TP*AP*AP*A)-3'; Telomere binding protein…
- UniProt
- Q84ZU4
- Pockets
- 5 · best druggability 0.54
Structure
x-ray diffraction · 4 distinct chains · 61% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, E | 5'-D(P*TP*TP*TP*AP*GP*GP*G)-3' | dna | 7 | — | — |
| D, F | 5'-D(P*CP*CP*CP*TP*AP*AP*A)-3' | dna | 7 | — | — |
| A | Telomere binding protein TBP1 | protein | 86 | 60% helix, 0% strand | Q84ZU4 |
| B | Telomere binding protein TBP1 | protein | 85 | 61% helix, 0% strand | Q84ZU4 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 244 | 0.54 | 0.77 | 26 | empty |
| 2 | 215 | 0.51 | 0.76 | 26 | empty |
| 3 | 220 | 0.51 | 0.76 | 24 | empty |
| 4 | 124 | 0.42 | 0.76 | 15 | empty |
| 5 | 113 | 0.38 | 0.75 | 14 | empty |
Interfaces
7 interfaces between chains.
- A–B · 343 Ų buried · 4 hydrogen bonds · protein-protein
- E–A · 338 Ų buried · 6 hydrogen bonds · protein-nucleic
- C–B · 332 Ų buried · 10 hydrogen bonds · protein-nucleic
- F–A · 324 Ų buried · 12 hydrogen bonds · protein-nucleic
- C–D · 316 Ų buried · 32 hydrogen bonds · nucleic-nucleic
Compared structures
- 2QHB · Crystal structure of NgTRF complexed with telomeric DNA · the same entry in another collection · chain D against D, 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 Q84ZU4
- Elsewhere: RCSB PDB 2QHB · PDBe 2QHB · UniProt Q84ZU4
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