4PKI: Actin, alpha skeletal muscle

Complex of ATP-actin With the C-terminal Actin-Binding Domain of Tropomodulin. Determined by X-ray diffraction at 2.3 Å resolution. Released 30 Jul 2014.

Method
X-ray diffraction
Resolution
2.3 Å
Organisms
Oryctolagus cuniculus, Homo sapiens
Chains
2
Atoms
5,617
Mol. weight
78.78 kDa
Ligands
CA, ATP
Released
30 Jul 2014

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

Secondary structure: helices and β-sheets

4PKI contains 38 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
β-strand8-1251
β-strand16-2161
β-strand2212
β-strand2412
β-strand29-3241
β-strand35-3843
α-helix45-473
β-strand53-5423
α-helix56-605
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-helix206-21611
α-helix223-23210
β-strand238-24146
β-strand247-25046
α-helix253-26210
α-helix264-2674
α-helix272-2732
α-helix274-28310
α-helix287-2893
α-helix290-2945
β-strand297-30045
α-helix302-3043
α-helix309-32012
β-strand329-33025
α-helix338-34811
β-strand357-35821
α-helix359-3657
α-helix367-3693
α-helix370-3734
Chain G: 15 helices, 12 β-strands
ElementResiduesLengthSheet
α-helix57-615
β-strand67-7487
β-strand77-8047
α-helix81-822
α-helix83-853
β-strand88-9038
β-strand94-10297
α-helix1071
β-strand108-11697
α-helix122-13817
β-strand144-14967
α-helix155-1584
β-strand166-16838
α-helix172-1743
α-helix1177-11782
α-helix1183-11919
β-strand1199-120139
α-helix1210-122011
β-strand1228-123039
α-helix1238-124811
β-strand1256-125839
α-helix1266-12749
α-helix1276-12783
β-strand1284-128639
α-helix1296-130611
β-strand1314-131639
α-helix1322-134524

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin, alpha skeletal muscleAprotein377Oryctolagus cuniculusP68135 (AlphaFold model)
Gelsolin,Tropomodulin-1 chimeraGprotein324Homo sapiensP06396 (AlphaFold model), P28289 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4PKI_1 Actin, alpha skeletal muscle (chains A)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF
Sequence of entity 2 (G), FASTA
>4PKI_2 Gelsolin,Tropomodulin-1 chimera (chains G)
MVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYD
LHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGG
VASGFGGSGGSGGSGLNSVIKPTQYKPVPDEEPNSTDVEETLERIKNNDPKLEEVNLNNI
RNIPIPTLKAYAEALKENSYVKKFSIVGTRSNDPVAYALAEMLKENKVLKTLNVESNFIS
GAGILRLVEALPYNTSLVEMKIDNQSQPLGNKVEMEIVSMLEKNATLLKFGYHFTQQGPR
LRASNAMMNNNDLVRKRRLADLTG

Ligands and cofactors

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

Primary citation

Actin cytoskeleton. Mechanism of actin filament pointed-end capping by tropomodulin. Rao, J.N., Madasu, Y., Dominguez, R. Science (2014) 345:463-467. DOI 10.1126/science.1256159 · PubMed

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

Browse structure collections

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