Solution Structure of the SWI1 ARID. Determined by solution NMR. Released 25 May 2004.
Explore 1RYU in 3D Show helices and sheets RCSB PDB PDBe
1RYU contains 6 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-13 | 3 | |
| α-helix | 19-34 | 16 | |
| α-helix | 52-62 | 11 | |
| α-helix | 67-69 | 3 | |
| α-helix | 73-80 | 8 | |
| α-helix | 88-100 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1 | A | protein | 120 | Homo sapiens | O14497 (AlphaFold model) |
>1RYU_1 SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1 (chains A) SSTTTNEKITKLYELGGEPERKMWVDRYLAFTEEKAMGMTNLPAVGRKPLDLYRLYVSVK EIGGLTQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQCLYAFECKIERGEDPPPDIFA
Structure and DNA-binding sites of the SWI1 AT-rich interaction domain (ARID) suggest determinants for sequence-specific DNA recognition. Kim, S., Zhang, Z., Upchurch, S. et al. J Biol Chem (2004) 279:16670-16676. DOI 10.1074/jbc.M312115200 · PubMed
Other PDB entries of the same protein (UniProt O14497 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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