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Crystal Structure of UP1 Complexed With d(TTAGGGTTAG(2PR)G); A Human Telomeric Repeat Containing 2-aminopurine
Analyse Crystal Structure of UP1 Complexed With d(TTAGGGTTAG(2PR)G); A Human Telomeric… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1U1R
- Type
- protein + DNA
- Length
- 194 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Homo sapiens; SYNTHETIC CONSTRUCT
- Molecule
- 5'-D(*TP*AP*GP*GP*GP*TP*TP*AP*GP*(2PR)P*G)-3'; Heterogeneous nuclear ribonucleoprotein A1
- UniProt
- P09651
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · resolution 1.8 · 2 distinct chains · 28% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | 5'-D(*TP*AP*GP*GP*GP*TP*TP*AP*GP*(2PR)P*G)-3' | dna | 11 | — | — |
| A | Heterogeneous nuclear ribonucleoprotein A1 | protein | 183 | 28% helix, 34% strand | P09651 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 185 | 0.54 | 0.78 | 21 | empty |
Interfaces
1 interface between chains.
- B–A · 791 Ų buried · 23 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 1 modified (nucleotide modification).
Compared structures
- 1U1R · Crystal structure of UP1 complexed with D(TTAGGGTTAG(2PR) G); a human telomeric repeat… · the same entry in another collection · chain A against A, TM-score 1.00
- P09651 · AlphaFold monomer V2.0 prediction for heterogeneous nuclear ribonucleoprotein A1 (P09651) · 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 P09651
- Elsewhere: RCSB PDB 1U1R · PDBe 1U1R · UniProt P09651
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