2HD7: C-teminal domain of twinfilin-1

Solution structure of C-teminal domain of twinfilin-1. Determined by solution NMR. Released 6 Feb 2007.

Method
Solution NMR
Organism
Mus musculus
Chains
1
Atoms
1,170
Mol. weight
16.64 kDa
Released
6 Feb 2007

Explore 2HD7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2HD7 contains 7 α-helices and 6 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: 7 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix1811
β-strand18211
α-helix1831
α-helix184-19310
β-strand200-20671
β-strand211-21661
α-helix225-2273
β-strand235-245111
β-strand248-258111
α-helix266-28116
α-helix282-2865
β-strand291-29771
α-helix305-3128

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Twinfilin-1Aprotein142Mus musculusQ91YR1 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2HD7_1 Twinfilin-1 (chains A)
AQGVAFPISRDAFQALEKLSKKQLNYVQLEIDIKNETIILANTENTELRDLPKRIPKDSA
RYHFFLYKHSHEGDYLESVVFIYSMPGYTCSIRERMLYSSCKSPLLEIVERQLQMDVIRK
IEIDNGDELTADFLYDEVHPKQ

Primary citation

Structural basis and evolutionary origin of actin filament capping by twinfilin. Paavilainen, V.O., Hellman, M., Helfer, E. et al. Proc Natl Acad Sci U S A (2007) 104:3113-3118. DOI 10.1073/pnas.0608725104 · PubMed

Other PDB entries of the same protein (UniProt Q91YR1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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