MolNFT v1 · #25621 · protein + DNA
HTRF2 DNA-binding domain in complex with telomeric DNA.
1W0U · Telomeric repeat binding factor 2: “HTRF2 DNA-binding domain in complex with telomeric DNA.”. X-ray diffraction, 2 pockets (best druggability 0.34). MolNFT v1 #25621 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1W0U
- Type
- protein + DNA
- Length
- 143 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Telomeric repeat binding factor 2; 5'-D(*TP*CP*TP*AP*GP*GP*GP*TP*TP*AP…
- UniProt
- Q15554
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · 3 distinct chains · 62% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Telomeric repeat binding factor 2 | protein | 55 | 62% helix, 0% strand | Q15554 |
| C | 5'-D(*TP*CP*TP*AP*GP*GP*GP*TP*TP*AP *GP*GP*GP*TP*TP*AP*G)-3' | dna | 16 | — | — |
| D | 5'-D(*CP*TP*AP*AP*CP*CP*CP*TP*AP*AP *CP*CP*CP*TP*AP*GP*A)-3' | dna | 17 | — | — |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.34 | 0.78 | 9 | empty |
| 2 | 59 | 0.32 | 0.77 | 13 | empty |
Interfaces
5 interfaces between chains.
- C–D · 718 Ų buried · 58 hydrogen bonds · nucleic-nucleic
- A–D · 464 Ų buried · 10 hydrogen bonds · protein-nucleic
- B–D · 434 Ų buried · 8 hydrogen bonds · protein-nucleic
- A–C · 414 Ų buried · 9 hydrogen bonds · protein-nucleic
- B–C · 400 Ų buried · 9 hydrogen bonds · protein-nucleic
Compared structures
- 1W0U · hTRF2 DNA-binding domain in complex with telomeric DNA. · the same entry in another collection · chain A against A, TM-score 1.00
- Q15554 · AlphaFold monomer V2.0 prediction for telomeric repeat-binding factor 2 (Q15554) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q15554
- Elsewhere: RCSB PDB 1W0U · PDBe 1W0U · UniProt Q15554
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