7ALN: Actin-1

Cryo-EM structure of the divergent actomyosin complex from Plasmodium falciparum Myosin A in the Rigor state. Determined by electron microscopy at 3.77 Å resolution. Released 28 Apr 2021.

Method
Electron microscopy
Resolution
3.77 Å
Organism
Plasmodium falciparum (isolate 3D7)
Chains
6
Atoms
20,789
Mol. weight
306.47 kDa
Ligands
ADP, MG, 9UE
Released
28 Apr 2021

Explore 7ALN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7ALN contains 140 α-helices and 125 β-strands across 6 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, C and E: 21 helices, 20 β-strands

ElementResiduesLengthSheet
β-strand9-1351
β-strand18-2251
β-strand30-3231
β-strand36-3942
β-strand4313
β-strand54-5522
α-helix57-615
α-helix63-653
β-strand66-6942
β-strand72-7324
β-strand76-7724
α-helix80-889
α-helix89-957
β-strand104-10851
α-helix114-1229
α-helix123-1275
β-strand13215
β-strand133-13751
α-helix138-1458
β-strand150-15456
β-strand163-16756
β-strand170-17126
α-helix183-19715
α-helix204-21714
α-helix224-2307
β-strand239-24247
β-strand248-25147
α-helix253-2553
α-helix260-2623
α-helix265-2673
α-helix275-28410
α-helix291-2955
β-strand298-30036
α-helix303-3053
α-helix310-32112
β-strand330-33126
α-helix339-34810
α-helix353-3553
β-strand35915
α-helix360-3667
α-helix367-3726
Chains B and D: 21 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand9-1358
β-strand18-2258
β-strand30-3238
β-strand36-3949
β-strand54-5529
α-helix57-615
α-helix63-653
β-strand66-6949
β-strand72-73210
β-strand76-77210
α-helix80-889
α-helix89-957
β-strand104-10858
α-helix114-1229
α-helix123-1275
β-strand132111
β-strand133-13758
α-helix138-1458
β-strand150-15453
β-strand163-16753
β-strand170-17123
α-helix183-19715
α-helix204-21714
α-helix224-2307
β-strand239-242412
β-strand248-251412
α-helix253-2553
α-helix260-2623
α-helix265-2673
α-helix275-28410
α-helix291-2955
β-strand298-30033
α-helix303-3053
α-helix310-32112
β-strand330-33123
α-helix339-34810
α-helix353-3553
β-strand359111
α-helix360-3667
α-helix367-3726
Chain F: 35 helices, 27 β-strands
ElementResiduesLengthSheet
α-helix5-1410
α-helix20-223
β-strand24131
β-strand31131
β-strand35-38432
α-helix42-465
β-strand53-57532
α-helix581
β-strand66-72732
β-strand80-82332
β-strand87-88232
α-helix102-1043
α-helix110-12213
β-strand127-128233
β-strand133-137533
α-helix148-1569
α-helix1641
α-helix167-18014
β-strand185-191733
α-helix197-20913
α-helix220-2267
α-helix228-2358
β-strand236-239434
β-strand242-246534
β-strand249-256833
α-helix2571
β-strand262-270933
β-strand287134
α-helix289-2968
α-helix299-3057
α-helix331-34010
α-helix346-36217
β-strand367-369335
β-strand379-381335
α-helix386-39510
α-helix400-4089
β-strand409-413536
β-strand418-422536
α-helix425-45531
β-strand465-470633
α-helix481-51131
α-helix516-5183
α-helix525-5328
α-helix538-54710
α-helix554-56310
β-strand570-572337
β-strand580-585637
β-strand588-593637
α-helix597-6015
α-helix607-6148
α-helix619-6246
α-helix641-65717
β-strand660-667833
α-helix680-68910
α-helix692-6998
β-strand705-708438
α-helix709-7157
α-helix721-7244
α-helix731-74111
β-strand749-751338
β-strand755-758438
α-helix760-7667

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin-1A, B, C, D, Eprotein376Plasmodium falciparum (isolate 3D7)Q8I4X0 (AlphaFold model)
Myosin-AFprotein818Plasmodium falciparum (isolate 3D7)Q8IDR3 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E), FASTA
>7ALN_1 Actin-1 (chains A, B, C, D, E)
MGEEDVQALVVDNGSGNVKAGVAGDDAPRSVFPSIVGRPKNPGIMVGMEEKDAFVGDEAQ
TKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRAAPEEHPVLLTEAPLNPKGNRERM
TQIMFESFNVPAMYVAIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIYEGYALPHAIMRLD
LAGRDLTEYLMKILHERGYGFSTSAEKEIVRDIKEKLCYIALNFDEEMKTSEQSSDIEKS
YELPDGNIITVGNERFRCPEALFQPSFLGKEAAGIHTTTFNSIKKCDVDIRKDLYGNIVL
SGGTTMYEGIGERLTRDITTLAPSTMKIKVVAPPERKYSVWIGGSILSSLSTFQQMWITK
EEYDESGPSIVHRKCF
Sequence of entity 2 (F), FASTA
>7ALN_2 Myosin-A (chains F)
MAVTNEEIKTASKIVRRVSNVEAFDKSGSVFKGYQIWTDISPTIENDPNIMFVKCVVQQG
SKKEKLTVVQIDPPGTGTPYDIDPTHAWNCNSQVDPMSFGDIGLLNHTNIPCVLDFLKHR
YLKNQIYTTAVPLIVAINPYKDLGNTTNEWIRRYRDTADHTKLPPHVFTCAREALSNLHG
VNKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLRIQTAIMAANPVLEAFGNAKTI
RNNNSSRFGRFMQLVISHEGGIRYGSVVAFLLEKSRIITQDDNERSYHIFYQFLKGANST
MKSKFGLKGVTEYKLLNPNSTEVSGVDDVKDFEEVIESLKNMELSESDIEVIFSIVAGIL
TLGNVRLIEKQEAGLSDAAAIMDEDMGVFNKACELMYLDPELIKREILIKVTVAGGDKIE
GRWNKNDAEVLKSSLCKAMYEKLFLWIIRHLNSRIEPEGGFKTFMGMLDIFGFEVFKNNS
LEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTAELKYTSNKEVINVLCEKGKSVLS
YLEDQCLAPGGTDEKFVSSCATNLKENNKFTPAKVASNKNFIIQHTIGPIQYCAESFLLK
NKDVLRGDLVEVIKDSPNPIVQQLFEGQVIEKGKIAKGSLIGSQFLNQLTSLMNLINSTE
PHFIRCIKPNENKKPLEWCEPKILIQLHALSILEALVLRQLGYSYRRTFEEFLYQYKFVD
IAAAEDSSVENQNKCVNILKLSGLSESMYKIGKSMVFLKQEGAKILTKIQREKLVEWENC
VSVIEAAILKHKYKQKVNKNIPSLLRVQAHIRKKMVAQ

Ligands and cofactors

IDNameFormulaCopies
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P25
MGMagnesium ionMg5
9UEJasplakinolideC36 H45 Br N4 O63

Primary citation

The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity. Robert-Paganin, J., Xu, X.P., Swift, M.F. et al. Nat Commun (2021) 12:1892-1892. DOI 10.1038/s41467-021-22093-4 · PubMed

Other PDB entries of the same protein (UniProt Q8I4X0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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