3TRV: L-Villin-1

Crystal structure of quasiracemic villin headpiece subdomain containing (F5Phe17) substitution. Determined by X-ray diffraction at 1.0 Å resolution. Released 25 Jan 2012.

Method
X-ray diffraction
Resolution
1.0 Å
Organism
Gallus gallus
Chains
2
Atoms
723
Mol. weight
8.67 kDa
Ligands
IPA
Released
25 Jan 2012

Explore 3TRV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3TRV contains 6 α-helices and 0 β-strands across 2 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 B: 3 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix3-108
α-helix14-185
α-helix22-309

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
L-Villin-1Aprotein35Gallus gallusP02640 (AlphaFold model)
D-Villin-1Bprotein35Gallus gallusP02640 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3TRV_1 L-Villin-1 (chains A)
LSDEDFKAVFGMTRSAFANLPLWKQQHLKKEKGLF
Sequence of entity 2 (B), FASTA
>3TRV_2 D-Villin-1 (chains B)
LSDEDFKAVFGMTRSAFANLPLWKQQHLKKEKGLF

Ligands and cofactors

IDNameFormulaCopies
IPAIsopropyl alcoholC3 H8 O2

Water and common crystallization additives (SO4) are not listed.

Primary citation

Quasiracemic crystallization as a tool to assess the accommodation of noncanonical residues in nativelike protein conformations. Mortenson, D.E., Satyshur, K.A., Guzei, I.A. et al. J Am Chem Soc (2012) 134:2473-2476. DOI 10.1021/ja210045s · 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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