5WFN: Actin-5C

Revised model of leiomodin 2-mediated actin regulation (alternate refinement of PDB 4RWT). Determined by X-ray diffraction at 3.0 Å resolution. Released 30 Aug 2017.

Method
X-ray diffraction
Resolution
3.0 Å
Organisms
Drosophila melanogaster, Homo sapiens
Chains
4
Atoms
8,906
Mol. weight
200.34 kDa
Ligands
MG, ANP
Released
30 Aug 2017

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

Secondary structure: helices and β-sheets

5WFN contains 60 α-helices and 52 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.

Chains A and B: 21 helices, 20 β-strands

ElementResiduesLengthSheet
β-strand8-1251
β-strand17-2151
β-strand2412
β-strand29-3131
β-strand35-3843
β-strand53-5423
α-helix56-594
α-helix62-643
β-strand65-6843
β-strand71-7224
β-strand75-7624
α-helix79-879
α-helix88-947
α-helix98-1003
β-strand103-10751
α-helix113-1219
α-helix122-1265
β-strand131-13661
α-helix137-1448
β-strand150-15565
β-strand160-16675
β-strand169-17025
β-strand176-17835
α-helix182-19615
α-helix203-21614
α-helix223-23210
β-strand238-24146
β-strand247-25046
α-helix252-26211
α-helix264-2674
α-helix274-28310
α-helix290-2945
β-strand297-30045
α-helix302-3043
α-helix309-32012
β-strand329-33025
α-helix338-34811
α-helix350-3523
β-strand357-35821
α-helix359-3657
α-helix367-3704
Chains C and D: 9 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix199-20810
β-strand215-21737
α-helix226-23712
β-strand244-24637
α-helix254-26613
β-strand272-27437
α-helix282-29110
α-helix292-2943
β-strand300-30237
α-helix312-32211
β-strand330-33237
α-helix338-36326
α-helix520-53011
α-helix534-5363
β-strand53812

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin-5CA, Bprotein384Drosophila melanogasterP10987 (AlphaFold model)
Leiomodin-2C, Dprotein506Homo sapiensQ6P5Q4 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5WFN_1 Actin-5C (chains A, B)
MCDEEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ
SKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKM
TQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLD
LAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKS
YELPDGQVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIREDLYANTVL
SGGTTMYPGIADRMQKEITALAKSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISK
QEYDESGPSIVHRKCFASHHHHHH
Sequence of entity 2 (C, D), FASTA
>5WFN_2 Leiomodin-2 (chains C, D)
MAHHHHHHVGTMSTFGYRRGLSKYESIDEDELLASLSAEELKELERELEDIEPDRNLPVG
LRQKSLTEKTPTGTFSREALMAYWEKESQKLLEKERLGECGKVAEDKEEEEDSDEEERTI
ETAKGINGTVNYDSVNSDNSKPKIFKSQIENINLTNGSNGRNTESPAAIHPCGNPTVIED
ALDKIKSNDPDTTEVNLNNIENITTQTLTRFAEALKDNTVVKTFSLANTHADDSAAMAIA
EMLKVNEHITNVNVESNFITGKGILAIMRALQHNTVLTELRFHNQRHIMGSQVEMEIVKL
LKENTTLLRLGYHFELPGPRMSMTSILTRNMDKQRQKRLQEQKQQEGYDGGPNLRTKVWQ
RGTPSSSPYVSPRHSPWSSPKLPKKVQTVRSRPLSPVATPPPPPPPPLPEKKLITRNIAE
VIKQQESAQRALQNGQGSGSGGSVGSQPNSILKEIKNSLRSVQEKKMEDSSRPSTPQRSA
HENLMEAIRGSSIKQLKRVEVPEALR

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg2
ANPPhosphoaminophosphonic acid-adenylate esterC10 H17 N6 O12 P32

Primary citation

Crystal structure of leiomodin 2 in complex with actin: a structural and functional reexamination. Boczkowska, M., Yurtsever, Z., Rebowski, G. et al. Biophys J (2017) 113:889-899. DOI 10.1016/j.bpj.2017.07.007

Other PDB entries of the same protein (UniProt P10987 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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