4Z94: Actin, alpha skeletal muscle

Actin Complex With a Chimera of Tropomodulin-1 and Leiomodin-1 Actin-Binding Site 2. Determined by X-ray diffraction at 2.4 Å resolution. Released 21 Oct 2015.

Method
X-ray diffraction
Resolution
2.4 Å
Organisms
Oryctolagus cuniculus, Homo sapiens
Chains
2
Atoms
5,582
Mol. weight
79.27 kDa
Ligands
CA, ATP
Released
21 Oct 2015

Explore 4Z94 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4Z94 contains 36 α-helices and 33 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.

Chain A: 23 helices, 21 β-strands

ElementResiduesLengthSheet
α-helix6-72
β-strand8-1251
β-strand16-2161
β-strand2212
β-strand2412
β-strand29-3241
β-strand35-3843
α-helix391
β-strand53-5423
α-helix55-606
β-strand65-6843
β-strand71-7224
β-strand75-7624
α-helix79-879
α-helix88-936
α-helix98-1003
β-strand103-10751
α-helix113-12513
β-strand131-13661
α-helix137-1448
β-strand150-15565
β-strand160-16675
β-strand169-17025
α-helix172-1743
β-strand176-17835
α-helix182-19413
α-helix203-21614
α-helix223-23210
β-strand238-24146
β-strand247-25046
α-helix253-2564
α-helix259-2624
α-helix264-2674
α-helix274-28310
α-helix290-2956
β-strand297-30045
α-helix302-3043
α-helix309-32012
β-strand329-33025
α-helix338-3469
α-helix350-3545
β-strand357-35821
α-helix359-3657
α-helix369-3735
Chain G: 13 helices, 12 β-strands
ElementResiduesLengthSheet
α-helix6-105
β-strand16-2387
β-strand26-2947
α-helix30-312
α-helix32-343
β-strand37-3938
β-strand43-5197
β-strand57-6597
α-helix71-8717
β-strand92-9877
α-helix104-1074
β-strand115-11738
α-helix121-1233
α-helix1183-11919
β-strand1199-120139
α-helix1210-122011
β-strand1228-136539
α-helix1373-138513
β-strand1391-139339
α-helix1401-141010
α-helix1411-14133
β-strand1419-142139
α-helix1431-144010
β-strand1449-145139
α-helix1457-148226

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin, alpha skeletal muscleAprotein377Oryctolagus cuniculusP68135 (AlphaFold model)
Gelsolin, Tropomodulin-1, Leiomodin-1 chimeraGprotein326Homo sapiensP06396 (AlphaFold model), P28289 (AlphaFold model), P29536 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4Z94_1 Actin, alpha skeletal muscle (chains A)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF
Sequence of entity 2 (G), FASTA
>4Z94_2 Gelsolin, Tropomodulin-1, Leiomodin-1 chimera (chains G)
MVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYD
LHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGG
VASGFGGSGGSGGSGLNSVIKPTQYKPVPDEEPNSTDVEETLERIKNNDPKLEEVNLNNI
RNIPIPTLKAYAEALKENSYVKKFALANTRADDHVAFAIAIMLKANKTITSLNLDSNHIT
GKGILAIFRALLQNNTLTELRFHNQRHICGGKTEMEIAKLLKENTTLLKLGYHFELAGPR
MTVTNLLSRNMDKQRQKRLQEQRQAQ

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa3
ATPAdenosine-5'-triphosphateC10 H16 N5 O13 P31

Primary citation

How Leiomodin and Tropomodulin use a common fold for different actin assembly functions. Boczkowska, M., Rebowski, G., Kremneva, E. et al. Nat Commun (2015) 6:8314-8314. DOI 10.1038/ncomms9314 · PubMed

Other PDB entries of the same protein (UniProt P68135 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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