2A40: Actin, alpha skeletal muscle

Ternary complex of the WH2 domain of WAVE with Actin-DNAse I. Determined by X-ray diffraction at 1.8 Å resolution. Released 1 Nov 2005.

Method
X-ray diffraction
Resolution
1.8 Å
Organisms
Oryctolagus cuniculus, Bos taurus
Chains
6
Atoms
11,357
Mol. weight
151.84 kDa
Ligands
CA, ATP, MG
Released
1 Nov 2005

Explore 2A40 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2A40 contains 80 α-helices and 80 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.

Chain A: 23 helices, 21 β-strands

ElementResiduesLengthSheet
β-strand8-1251
β-strand16-2161
β-strand2412
β-strand29-3241
β-strand35-3843
β-strand42-4434
β-strand53-5423
α-helix56-605
α-helix62-643
β-strand65-6843
β-strand71-7225
β-strand75-7625
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-strand150-15566
β-strand160-16676
β-strand169-17026
α-helix172-1743
β-strand176-17836
α-helix182-19615
α-helix203-21614
α-helix223-23210
β-strand238-24147
β-strand247-25047
α-helix253-26210
α-helix264-2674
α-helix274-28411
α-helix287-2948
β-strand297-30046
α-helix302-3043
α-helix309-32012
β-strand329-33026
α-helix335-3373
α-helix338-34811
α-helix350-3556
α-helix3561
β-strand357-35821
α-helix359-3646
Chain B: 14 helices, 18 β-strands
ElementResiduesLengthSheet
β-strand2-11104
α-helix13-175
α-helix19-2911
β-strand34-4074
α-helix46-5510
β-strand64-6744
α-helix68-703
β-strand7118
β-strand7818
β-strand79-8464
β-strand90-9679
α-helix105-1084
α-helix112-1132
β-strand114-11969
β-strand127-13269
α-helix137-1393
α-helix140-15819
β-strand163-16869
α-helix178-1836
α-helix185-1884
β-strand192-19439
β-strand203110
β-strand212-21769
α-helix219-2246
β-strand225111
α-helix2261
β-strand231-23224
α-helix235-2384
α-helix243-2497
β-strand252110
β-strand255-25844
β-strand259111
Chain C: 3 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix435-44511
α-helix4491
β-strand45012
α-helix4511
Chain D: 23 helices, 21 β-strands
ElementResiduesLengthSheet
α-helix6-72
β-strand8-12512
β-strand16-21612
β-strand24113
β-strand29-32412
β-strand35-38414
β-strand42-44315
β-strand53-54214
α-helix56-605
α-helix62-643
β-strand65-68414
β-strand71-72216
β-strand75-76216
α-helix79-879
α-helix88-947
α-helix98-1003
β-strand103-107512
α-helix113-12513
β-strand131-136612
α-helix137-1448
β-strand150-155617
β-strand160-166717
β-strand169-170217
α-helix172-1743
β-strand176-178317
α-helix182-19615
α-helix203-21614
α-helix223-23210
β-strand238-241418
α-helix2461
β-strand247-250418
α-helix253-2597
α-helix264-2674
α-helix274-28310
α-helix287-2948
β-strand297-300417
α-helix302-3043
α-helix309-32012
β-strand329-330217
α-helix335-3373
α-helix338-34811
α-helix350-3556
β-strand357-358212
α-helix359-3646
Chain E: 14 helices, 18 β-strands
ElementResiduesLengthSheet
β-strand2-111015
α-helix13-164
α-helix19-2911
β-strand34-40715
α-helix46-5510
β-strand64-67415
α-helix68-703
β-strand71119
β-strand78119
β-strand79-84615
β-strand90-96720
α-helix104-1074
α-helix112-1132
β-strand114-119620
β-strand127-132620
α-helix137-1393
α-helix140-15819
β-strand163-168620
α-helix178-1836
α-helix185-1884
β-strand192-194320
β-strand203121
β-strand212-217620
α-helix219-2246
β-strand225122
α-helix2261
β-strand231-232215
α-helix235-2384
α-helix243-2497
β-strand252121
β-strand255-258415
β-strand259122
Chain F: 3 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix435-44511
α-helix4491
β-strand450113
α-helix451-4533

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin, alpha skeletal muscleA, Dprotein375Oryctolagus cuniculusP68135 (AlphaFold model)
Deoxyribonuclease-1B, Eprotein260Bos taurusP00639 (AlphaFold model)
Wiskott-Aldrich syndrome protein family member 2C, Fprotein32Q9Y6W5 (AlphaFold model)
Sequence of entity 1 (A, D), FASTA
>2A40_1 Actin, alpha skeletal muscle (chains A, D)
DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT
QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL
AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ
EYDEAGPSIVHRKCF
Sequence of entity 2 (B, E), FASTA
>2A40_2 Deoxyribonuclease-1 (chains B, E)
LKIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDP
NTYHYVVSEPLGRNSYKERYLFLFRPNKVSVLDTYQYDDGCESCGNDSFSREPAVVKFSS
HSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQ
WSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAYG
LSNEMALAISDHYPVEVTLT
Sequence of entity 3 (C, F), FASTA
>2A40_3 Wiskott-Aldrich syndrome protein family member 2 (chains C, F)
VSDARSDLLSAIRQGFQLRRVEEQREQEKRDV

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa4
ATPAdenosine-5'-triphosphateC10 H16 N5 O13 P32
MGMagnesium ionMg2

Water and common crystallization additives (GOL) are not listed.

Primary citation

Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly. Chereau, D., Kerff, F., Graceffa, P. et al. Proc Natl Acad Sci U S A (2005) 102:16644-16649. DOI 10.1073/pnas.0507021102 · 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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