3J0S: Actin, cytoplasmic 1

Remodeling of actin filaments by ADF cofilin proteins. Determined by electron microscopy at 9.0 Å resolution. Released 21 Dec 2011.

Method
Electron microscopy
Resolution
9.0 Å
Organisms
Gallus gallus, Homo sapiens
Chains
24
Atoms
50,556
Mol. weight
722.21 kDa
Released
21 Dec 2011

Explore 3J0S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3J0S contains 336 α-helices and 312 β-strands across 24 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, B, C, D, E, F, G, H, I, J, K and L: 20 helices, 19 β-strands

ElementResiduesLengthSheet
β-strand8-1141
β-strand17-2041
β-strand29-3131
β-strand35-3842
α-helix40-423
β-strand53-5422
α-helix57-604
β-strand65-6842
β-strand71-7223
β-strand75-7623
α-helix79-8810
α-helix89-946
β-strand103-10751
α-helix113-12513
β-strand131-13661
α-helix137-1448
β-strand149-15574
β-strand160-16674
β-strand169-17024
α-helix172-1743
β-strand176-17834
α-helix183-19614
α-helix203-2053
α-helix208-2169
α-helix223-23210
β-strand23815
β-strand25015
α-helix253-26210
α-helix264-2663
α-helix272-2732
α-helix274-28411
α-helix290-2956
β-strand297-30044
α-helix309-32012
β-strand329-33024
α-helix338-3458
β-strand357-35821
α-helix359-3657
α-helix369-3735
Chains M, N, O, P, Q, R, S, T, U, V, W and X: 8 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix10-2011
α-helix26-294
β-strand33-40861
β-strand47-561061
α-helix58-625
α-helix67-737
β-strand82-86561
β-strand90-92362
β-strand94-95262
β-strand99-104661
α-helix111-1199
α-helix121-1266
β-strand133-137561
α-helix140-1445
α-helix146-1538

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin, cytoplasmic 1A, B, C, D, E, F, G, H, I, J, K, Lprotein374Gallus gallusP60706 (AlphaFold model)
Cofilin-2M, N, O, P, Q, R, S, T, U, V, W, Xprotein166Homo sapiensP23528 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L), FASTA
>3J0S_1 Actin, cytoplasmic 1 (chains A, B, C, D, E, F, G, H, I, J, K, L)
DDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSK
RGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQ
IMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLA
GRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYE
LPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSG
GTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE
YDESGPSIVHRKCF
Sequence of entity 2 (M, N, O, P, Q, R, S, T, U, V, W, X), FASTA
>3J0S_2 Cofilin-2 (chains M, N, O, P, Q, R, S, T, U, V, W, X)
MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDV
GQTVDDPYATFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASS
KDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL

Primary citation

Remodeling of actin filaments by ADF/cofilin proteins. Galkin, V.E., Orlova, A., Kudryashov, D.S. et al. Proc Natl Acad Sci U S A (2011) 108:20568-20572. DOI 10.1073/pnas.1110109108 · PubMed

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