5I1S: Villin-1

Villin headpiece subdomain with a Lys30 to APC substitution. Determined by X-ray diffraction at 1.12 Å resolution. Released 25 May 2016.

Method
X-ray diffraction
Resolution
1.12 Å
Organisms
Gallus gallus, synthetic construct
Chains
4
Atoms
1,510
Mol. weight
16.31 kDa
Released
25 May 2016

Explore 5I1S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5I1S contains 12 α-helices and 0 β-strands across 4 chains. 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.

Chains A and D: 3 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix3-108
α-helix14-185
α-helix22-3110
Chains B and C: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix3-108
α-helix14-196
α-helix22-3110

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Villin-1A, Bprotein35Gallus gallusP02640 (AlphaFold model)
D-Villin headpiece subdomainC, Dprotein35synthetic construct
Sequence of entity 1 (A, B), FASTA
>5I1S_1 Villin-1 (chains A, B)
LSDEDFKAVFGMTRSAFANLPLWKQQHLKXEKGLF
Sequence of entity 2 (C, D), FASTA
>5I1S_2 D-Villin headpiece subdomain (chains C, D)
LSDEDFKAVFGMTRSAFANLPLWKQQHLKKEKGLF

Primary citation

Effects of Single alpha-to-beta Residue Replacements on Structure and Stability in a Small Protein: Insights from Quasiracemic Crystallization. Kreitler, D.F., Mortenson, D.E., Forest, K.T. et al. J Am Chem Soc (2016) 138:6498-6505. DOI 10.1021/jacs.6b01454 · PubMed

Other PDB entries of the same protein (UniProt P02640 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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