1RYU: SWI1 ARID

Solution Structure of the SWI1 ARID. Determined by solution NMR. Released 25 May 2004.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
953
Mol. weight
13.59 kDa
Released
25 May 2004

Explore 1RYU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 6 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix11-133
α-helix19-3416
α-helix52-6211
α-helix67-693
α-helix73-808
α-helix88-10013

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1Aprotein120Homo sapiensO14497 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1RYU_1 SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1 (chains A)
SSTTTNEKITKLYELGGEPERKMWVDRYLAFTEEKAMGMTNLPAVGRKPLDLYRLYVSVK
EIGGLTQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQCLYAFECKIERGEDPPPDIFA

Primary citation

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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