Research workbench
HTRF1 DNA-binding domain in complex with telomeric DNA.
Analyse HTRF1 DNA-binding domain in complex 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
- 1W0T
- Type
- protein + DNA
- Length
- 142 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Telomeric repeat binding factor 1; 5'-D(*CP*TP*GP*TP*TP*AP*GP*GP*GP*TP…
- UniProt
- P54274
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · 3 distinct chains · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Telomeric repeat binding factor 1 | protein | 52 | 63% helix, 0% strand | P54274 |
| C | 5'-D(*CP*TP*GP*TP*TP*AP*GP*GP*GP*TP *TP*AP*GP*GP*GP*TP*TP*AP*G)-3' | dna | 19 | — | — |
| D | 5'-D(*TP*CP*TP*AP*AP*CP*CP*CP*TP*AP *AP*CP*CP*CP*TP*AP*AP*CP*A)-3' | dna | 19 | — | — |
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 | 86 | 0.34 | 0.75 | 18 | empty |
| 2 | 50 | 0.26 | 0.74 | 9 | empty |
Interfaces
5 interfaces between chains.
- C–D · 811 Ų buried · 61 hydrogen bonds · nucleic-nucleic
- B–D · 470 Ų buried · 11 hydrogen bonds · protein-nucleic
- A–D · 467 Ų buried · 9 hydrogen bonds · protein-nucleic
- A–C · 413 Ų buried · 13 hydrogen bonds · protein-nucleic
- B–C · 396 Ų buried · 9 hydrogen bonds · protein-nucleic
Compared structures
- 1W0T · hTRF1 DNA-binding domain in complex with telomeric DNA. · the same entry in another collection · chain A against A, 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 0.96
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
- Elsewhere: RCSB PDB 1W0T · PDBe 1W0T · UniProt P54274
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