Research workbench
Crystal structure of the heterodimeric NPAS1-arnt complex
Analyse Crystal structure of the heterodimeric NPAS1-arnt complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5SY5
- Type
- protein
- Length
- 1,669 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P53762, P97459
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 278 | — | P53762 |
| B | — | protein | 278 | — | P97459 |
| C | — | protein | 269 | — | P53762 |
| D | — | protein | 283 | — | P97459 |
| E | — | protein | 279 | — | P53762 |
| F | — | protein | 282 | — | P97459 |
Compared structures
- 5SY5 · Crystal Structure of the Heterodimeric NPAS1-ARNT Complex · the same entry in another collection · chain F against F, TM-score 1.00
- P97459 · AlphaFold monomer V2.0 prediction for neuronal pas domain-containing protein 1 (P97459) · a predicted model of the same protein · chain B against A, TM-score 0.99
- P53762 · AlphaFold monomer V2.0 prediction for aryl hydrocarbon receptor nuclear translocator… · a predicted model of the same protein · chain A against A, TM-score 0.89
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 P53762
- Every structure of UniProt P97459
- Elsewhere: RCSB PDB 5SY5 · PDBe 5SY5 · UniProt P53762 · UniProt P97459
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