5YPU: Actin monomer

Crystal structure of an actin monomer in complex with the nucleator Cordon-Bleu MET72NLE WH2-motif peptide. Determined by X-ray diffraction at 2.0 Å resolution. Released 26 Sept 2018.

Method
X-ray diffraction
Resolution
2.0 Å
Organisms
Oryctolagus cuniculus, Mus musculus
Chains
4
Atoms
6,550
Mol. weight
88.07 kDa
Ligands
CA, ATP
Released
26 Sept 2018

Explore 5YPU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5YPU contains 51 α-helices and 42 β-strands across 4 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, 20 β-strands

ElementResiduesLengthSheet
β-strand8-1251
β-strand16-2161
β-strand2412
β-strand29-3241
β-strand3513
β-strand5413
α-helix56-605
β-strand6813
β-strand71-7224
β-strand75-7624
α-helix79-8810
α-helix89-935
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-helix182-19211
α-helix193-1964
α-helix203-21614
α-helix223-23210
β-strand238-24146
α-helix2461
β-strand247-25046
α-helix253-2597
α-helix264-2674
α-helix274-28310
α-helix287-2948
β-strand297-30045
α-helix302-3043
α-helix309-32012
β-strand329-33025
α-helix335-3373
α-helix338-34811
α-helix350-3556
β-strand357-35821
α-helix359-3657
α-helix367-3715
Chains B and D: 3 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix67-7610
α-helix80-834
β-strand8512
α-helix861
Chain C: 22 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand8-1257
β-strand16-2167
β-strand2418
β-strand29-3247
β-strand3519
β-strand5419
α-helix56-605
α-helix66-672
β-strand6819
β-strand71-72210
β-strand75-76210
α-helix79-879
α-helix88-936
α-helix98-1003
β-strand103-10757
α-helix113-12513
β-strand131-13667
α-helix137-1448
β-strand150-155611
β-strand160-166711
β-strand169-170211
α-helix172-1743
β-strand176-178311
α-helix182-19211
α-helix193-1964
α-helix203-21614
α-helix223-23210
β-strand238-241412
β-strand247-250412
α-helix253-2597
α-helix264-2674
α-helix274-28310
α-helix287-2948
β-strand297-300411
α-helix302-3043
α-helix309-32012
β-strand329-330211
α-helix338-34811
α-helix350-3556
β-strand357-35827
α-helix359-3657
α-helix367-3715

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin, alpha skeletal muscleA, Cprotein368Oryctolagus cuniculusP68135 (AlphaFold model)
Cordon-Bleu WH2 motifB, Dprotein22Mus musculusQ5NBX1 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>5YPU_1 Actin, alpha skeletal muscle (chains A, C)
TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGI
LTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMF
ETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRD
LTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPD
GQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTT
MYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDE
AGPSIVHR
Sequence of entity 2 (B, D), FASTA
>5YPU_2 Cordon-Bleu WH2 motif (chains B, D)
SLHSALLEAIHSSGGREKLRKV

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa7
ATPAdenosine-5'-triphosphateC10 H16 N5 O13 P32

Primary citation

Structural evidence for the roles of divalent cations in actin polymerization and activation of ATP hydrolysis. Scipion, C.P.M., Ghoshdastider, U., Ferrer, F.J. et al. Proc Natl Acad Sci U S A (2018) 115:10345-10350. DOI 10.1073/pnas.1806394115 · 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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