2A42: Actin-DNAse I Complex

Actin-DNAse I Complex. Determined by X-ray diffraction at 1.85 Å resolution. Released 1 Nov 2005.

Method
X-ray diffraction
Resolution
1.85 Å
Organisms
Oryctolagus cuniculus, Bos taurus
Chains
2
Atoms
5,546
Mol. weight
72.28 kDa
Ligands
MG, ATP, CA
Released
1 Nov 2005

Explore 2A42 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2A42 contains 36 α-helices and 38 β-strands across 2 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
α-helix6-72
β-strand8-1251
β-strand16-2161
β-strand29-3241
β-strand35-3842
β-strand42-4433
α-helix48-503
β-strand53-5422
α-helix56-605
α-helix62-643
β-strand65-6842
β-strand71-7224
β-strand75-7624
α-helix79-8810
α-helix89-946
α-helix98-1003
β-strand103-10751
α-helix113-12513
β-strand131-13661
α-helix137-1448
β-strand150-15565
β-strand160-16675
β-strand169-17025
α-helix172-1743
β-strand176-17835
α-helix182-19615
α-helix206-21611
α-helix223-23210
β-strand238-24146
β-strand247-25046
α-helix253-26210
α-helix264-2674
α-helix274-28310
α-helix287-2948
β-strand297-30045
α-helix302-3043
α-helix309-32012
β-strand329-33025
α-helix335-3373
α-helix338-34710
α-helix350-3545
β-strand357-35821
α-helix359-3646
Chain B: 13 helices, 18 β-strands
ElementResiduesLengthSheet
β-strand2-11103
α-helix13-164
α-helix19-2911
β-strand34-4073
α-helix46-5510
β-strand64-6743
α-helix68-703
β-strand7117
β-strand7817
β-strand79-8463
β-strand89-9688
α-helix112-1132
β-strand114-12078
β-strand127-13268
α-helix137-1393
α-helix140-15819
β-strand163-16868
α-helix178-1836
α-helix185-1884
β-strand192-19438
β-strand20319
β-strand212-21768
α-helix219-2246
β-strand225110
α-helix2261
β-strand231-23223
α-helix235-2384
α-helix243-2497
β-strand25219
β-strand255-25843
β-strand259110

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin, alpha skeletal muscleAprotein375Oryctolagus cuniculusP68135 (AlphaFold model)
Deoxyribonuclease-1Bprotein260Bos taurusP00639 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2A42_1 Actin, alpha skeletal muscle (chains A)
DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT
QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL
AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ
EYDEAGPSIVHRKCF
Sequence of entity 2 (B), FASTA
>2A42_2 Deoxyribonuclease-1 (chains B)
LKIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDP
NTYHYVVSEPLGRNSYKERYLFLFRPNKVSVLDTYQYDDGCESCGNDSFSREPAVVKFSS
HSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQ
WSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAYG
LSNEMALAISDHYPVEVTLT

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1
ATPAdenosine-5'-triphosphateC10 H16 N5 O13 P31
CACalcium ionCa2

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:

Browse structure collections

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