Research workbench
Crystal Structure of the NPAS4-ARNT2 heterodimer in complex with DNA
Analyse Crystal Structure of the NPAS4-ARNT2 heterodimer in complex with DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7XI3
- Type
- protein + DNA
- Length
- 633 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 4.274
- Source
- Mus musculus
- Molecule
- Aryl hydrocarbon receptor nuclear translocator 2; Neuronal PAS domain protein 4; DNA…
- UniProt
- A1L327
- Pockets
- 12 · best druggability 0.78
Structure
x-ray diffraction · resolution 4.274 · 4 distinct chains · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aryl hydrocarbon receptor nuclear translocator 2 | protein | 287 | 31% helix, 29% strand | — |
| B | Neuronal PAS domain protein 4 | protein | 314 | 34% helix, 24% strand | A1L327 |
| C | DNA (5'-D(P*GP*GP*AP*GP*GP*TP*CP*GP*TP*GP*AP*GP*TP*GP*AP*T)-3') | dna | 16 | — | — |
| D | DNA (5'-D(P*CP*CP*AP*TP*CP*AP*CP*TP*CP*AP*CP*GP*AP*CP*CP*T)-3') | dna | 16 | — | — |
Pockets
12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 232 | 0.78 | 0.92 | 27 | empty |
| 2 | 424 | 0.68 | 0.80 | 45 | empty |
| 3 | 119 | 0.62 | 0.86 | 22 | empty |
| 4 | 220 | 0.45 | 0.73 | 23 | empty |
| 5 | 59 | 0.43 | 0.82 | 17 | empty |
Interfaces
6 interfaces between chains.
- A–B · 3822 Ų buried · 27 hydrogen bonds · protein-protein
- C–D · 567 Ų buried · 29 hydrogen bonds · nucleic-nucleic
- A–C · 478 Ų buried · 10 hydrogen bonds · protein-nucleic
- B–D · 452 Ų buried · 10 hydrogen bonds · protein-nucleic
- A–D · 198 Ų buried · 5 hydrogen bonds · protein-nucleic
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 A1L327
- Elsewhere: RCSB PDB 7XI3 · PDBe 7XI3 · UniProt A1L327
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