4RWT: Actin-Lmod complex

Structure of actin-Lmod complex. Determined by X-ray diffraction at 2.98 Å resolution. Released 14 Oct 2015.

Method
X-ray diffraction
Resolution
2.98 Å
Organisms
Drosophila melanogaster, Homo sapiens
Chains
4
Atoms
9,317
Mol. weight
200.34 kDa
Ligands
ANP, MG
Released
14 Oct 2015

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

Secondary structure: helices and β-sheets

4RWT contains 67 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.

Chain A: 23 helices, 20 β-strands

ElementResiduesLengthSheet
β-strand8-1141
β-strand16-2161
β-strand29-3241
β-strand35-3842
α-helix44-463
β-strand53-5422
α-helix56-605
β-strand65-6842
β-strand71-7223
β-strand75-7623
α-helix79-879
α-helix88-936
β-strand103-10751
α-helix113-1219
α-helix122-1265
β-strand13114
β-strand132-13651
α-helix137-1448
β-strand150-15565
β-strand160-16675
β-strand169-17025
β-strand176-17835
α-helix182-19514
α-helix203-21614
α-helix223-23210
β-strand238-24146
β-strand247-25046
α-helix253-2564
α-helix259-2624
α-helix264-2674
α-helix272-2732
α-helix274-28310
α-helix290-2945
β-strand297-30045
α-helix302-3043
α-helix309-32012
β-strand329-33025
α-helix338-34811
α-helix350-3556
β-strand35814
α-helix359-3657
α-helix367-3693
α-helix370-3734
Chain B: 21 helices, 21 β-strands
ElementResiduesLengthSheet
β-strand8-11410
β-strand16-21610
β-strand2419
β-strand29-32410
β-strand35-38411
β-strand53-54211
α-helix56-605
β-strand65-68411
β-strand71-72212
β-strand75-76212
α-helix79-879
α-helix88-936
β-strand103-107510
α-helix113-1219
α-helix122-1265
β-strand131113
β-strand132-136510
α-helix137-1448
β-strand150-155614
β-strand160-166714
β-strand169-170214
β-strand176-178314
α-helix182-19514
α-helix203-21614
α-helix223-23210
β-strand238-241415
β-strand247-250415
α-helix253-2564
α-helix259-2624
α-helix264-2674
α-helix272-2732
α-helix274-28310
α-helix290-2945
β-strand297-300414
α-helix302-3043
α-helix309-32012
β-strand329-330214
α-helix338-34811
α-helix350-3556
β-strand358113
α-helix359-3657
α-helix367-3704
Chain C: 8 helices, 5 β-strands
ElementResiduesLengthSheet
α-helix167-17610
β-strand183-18537
α-helix194-20310
β-strand212-21657
α-helix222-23211
β-strand240-24457
α-helix250-25910
α-helix260-2623
β-strand268-27037
α-helix281-2899
α-helix290-2923
β-strand298-30037
α-helix306-33025
Chain D: 15 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix167-17610
β-strand183-18538
α-helix195-2039
β-strand212-21438
α-helix222-23312
β-strand240-24238
α-helix250-25910
α-helix260-2623
β-strand268-27038
α-helix281-2899
α-helix290-2923
β-strand298-30038
α-helix306-32722
α-helix328-3325
α-helix408-4169
α-helix438-4414
α-helix443-4453
α-helix468-47811
α-helix482-4843
β-strand48619
α-helix4871

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin-5CA, Bprotein384Drosophila melanogasterP10987 (AlphaFold model)
Leiomodin-2C, Dprotein506Homo sapiensQ6P5Q4 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4RWT_1 Actin-5C (chains A, B)
MCDEEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ
SKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKM
TQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLD
LAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKS
YELPDGQVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIREDLYANTVL
SGGTTMYPGIADRMQKEITALAKSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISK
QEYDESGPSIVHRKCFASHHHHHH
Sequence of entity 2 (C, D), FASTA
>4RWT_2 Leiomodin-2 (chains C, D)
MAHHHHHHVGTMSTFGYRRGLSKYESIDEDELLASLSAEELKELERELEDIEPDRNLPVG
LRQKSLTEKTPTGTFSREALMAYWEKESQKLLEKERLGECGKVAEDKEEEEDSDEEERTI
ETAKGINGTVNYDSVNSDNSKPKIFKSQIENINLTNGSNGRNTESPAAIHPCGNPTVIED
ALDKIKSNDPDTTEVNLNNIENITTQTLTRFAEALKDNTVVKTFSLANTHADDSAAMAIA
EMLKVNEHITNVNVESNFITGKGILAIMRALQHNTVLTELRFHNQRHIMGSQVEMEIVKL
LKENTTLLRLGYHFELPGPRMSMTSILTRNMDKQRQKRLQEQKQQEGYDGGPNLRTKVWQ
RGTPSSSPYVSPRHSPWSSPKLPKKVQTVRSRPLSPVATPPPPPPPPLPEKKLITRNIAE
VIKQQESAQRALQNGQGSGSGGSVGSQPNSILKEIKNSLRSVQEKKMEDSSRPSTPQRSA
HENLMEAIRGSSIKQLKRVEVPEALR

Ligands and cofactors

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

Primary citation

Mechanisms of leiomodin 2-mediated regulation of actin filament in muscle cells. Chen, X., Ni, F., Kondrashkina, E. et al. Proc Natl Acad Sci U S A (2015) 112:12687-12692. DOI 10.1073/pnas.1512464112 · PubMed

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

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