8D13: Helical ADP-F-actin

Helical ADP-F-actin. Determined by electron microscopy at 2.43 Å resolution. Released 7 Sept 2022.

Method
Electron microscopy
Resolution
2.43 Å
Organism
Gallus gallus
Chains
3
Atoms
9,216
Mol. weight
127.68 kDa
Ligands
MG, ADP
Released
7 Sept 2022

Explore 8D13 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8D13 contains 69 α-helices and 58 β-strands across 3 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: 23 helices, 19 β-strands

ElementResiduesLengthSheet
β-strand8-1251
β-strand16-2161
β-strand29-3241
β-strand35-3842
β-strand53-5422
α-helix56-605
α-helix62-643
β-strand65-6842
β-strand71-7223
β-strand75-7623
α-helix79-8810
α-helix89-935
α-helix98-1003
β-strand103-10751
α-helix113-12513
β-strand131-13661
α-helix137-1448
β-strand150-15564
β-strand160-16674
β-strand169-17024
α-helix172-1743
β-strand176-17834
α-helix182-19211
α-helix193-1964
α-helix203-21614
α-helix223-23210
β-strand238-24145
β-strand247-25045
α-helix253-2564
α-helix258-2614
α-helix264-2674
α-helix274-28310
α-helix290-2945
β-strand297-30044
α-helix302-3054
α-helix309-32012
β-strand329-33024
α-helix335-3373
α-helix338-34811
β-strand357-35821
α-helix359-3657
α-helix369-3735
Chain C: 23 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand8-12511
β-strand16-21611
β-strand29-32411
β-strand35-38412
β-strand41-4229
β-strand53-54212
α-helix56-605
α-helix62-643
β-strand65-68412
β-strand71-72213
β-strand75-76213
α-helix79-8810
α-helix89-935
α-helix98-1003
β-strand103-107511
α-helix113-12513
β-strand131-136611
α-helix137-1448
β-strand150-155614
β-strand160-166714
β-strand169-170214
α-helix172-1743
β-strand176-178314
α-helix182-19211
α-helix193-1964
α-helix203-21614
α-helix223-23210
β-strand238-241415
β-strand247-250415
α-helix253-2564
α-helix258-2614
α-helix264-2674
α-helix274-28310
α-helix290-2945
β-strand297-300414
α-helix302-3054
α-helix309-32012
β-strand329-330214
α-helix335-3373
α-helix338-34811
β-strand357-358211
α-helix359-3657
α-helix369-3735

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin, alpha skeletal muscleA, B, Cprotein377Gallus gallusP68139 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>8D13_1 Actin, alpha skeletal muscle (chains A, B, C)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg3
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P23

Primary citation

Bending forces and nucleotide state jointly regulate F-actin structure. Reynolds, M.J., Hachicho, C., Carl, A.G. et al. Nature (2022) 611:380-386. DOI 10.1038/s41586-022-05366-w · PubMed

Other PDB entries of the same protein (UniProt P68139 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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