6RSW: HFD domain of mouse CAP1

HFD domain of mouse CAP1 bound to the pointed end of G-actin. Determined by X-ray diffraction at 1.95 Å resolution. Released 27 Nov 2019.

Method
X-ray diffraction
Resolution
1.95 Å
Organisms
Oryctolagus cuniculus, Mus musculus
Chains
3
Atoms
6,145
Mol. weight
78.7 kDa
Ligands
MG, ADP
Released
27 Nov 2019

Explore 6RSW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6RSW contains 39 α-helices and 25 β-strands across 3 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, 19 β-strands

ElementResiduesLengthSheet
α-helix6-72
β-strand8-1251
β-strand16-2161
β-strand29-3241
β-strand35-3842
β-strand53-5422
α-helix56-605
α-helix62-643
β-strand65-6842
β-strand71-7223
β-strand75-7623
α-helix79-8810
α-helix89-946
α-helix98-1003
β-strand103-10751
α-helix113-1219
α-helix122-1265
β-strand131-13661
α-helix137-1448
β-strand150-15564
β-strand160-16674
β-strand169-17024
α-helix172-1743
β-strand176-17834
α-helix182-19615
α-helix203-21614
α-helix223-23210
β-strand238-24145
β-strand247-25045
α-helix253-26210
α-helix264-2674
α-helix274-28411
α-helix287-2948
β-strand297-30044
α-helix302-3043
α-helix309-32012
β-strand329-33024
α-helix338-34811
α-helix350-3545
β-strand357-35821
α-helix359-3657
α-helix369-3724
Chain B: 7 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix180-1812
β-strand18216
α-helix1831
α-helix184-19411
β-strand200-20676
β-strand211-21666
α-helix222-2287
β-strand235-245116
β-strand248-258116
α-helix266-28722
β-strand291-29776
α-helix300-3023
α-helix305-3128
Chain C: 9 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix41-499
α-helix50-545
α-helix55-6410
α-helix66-9025
α-helix97-11923
α-helix127-1348
α-helix137-1448
α-helix149-17123
α-helix176-19924

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin, alpha skeletal muscleAprotein375Oryctolagus cuniculusP68135 (AlphaFold model)
Twinfilin-1Bprotein141Mus musculusQ91YR1 (AlphaFold model)
Adenylyl cyclase-associated protein 1Cprotein172Mus musculusP40124 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6RSW_1 Actin, alpha skeletal muscle (chains A)
DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT
QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL
AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ
EYDEAGPSIVHRKCF
Sequence of entity 2 (B), FASTA
>6RSW_2 Twinfilin-1 (chains B)
QGVAFPISRDAFQALEKLSKKQLNYVQLEIDIKNETIILANTENTELRDLPKRIPKDSAR
YHFFLYKHSHEGDYLESVVFIYSMPGYTCSIRERMLYSSCKSPLLEIVERQLQMDVIRKI
EIDNGDELTADFLYDEVHPKQ
Sequence of entity 3 (C), FASTA
>6RSW_3 Adenylyl cyclase-associated protein 1 (chains C)
AVPYVQAFDSLLANPVAEYLKMSKEIGGDVQKHAEMVHTGLKLERALLATASQSQQPAGN
KLSDLLAPISEQIQEVITFREKNRGSKFFNHLSAVSESIQALGWVALAAKPGPFVKEMND
AAMFYTNRVLKEYRDVDKKHVDWVRAYLSIWTELQAYIKEFHTTGLAWSKTG

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg2
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P21

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

Primary citation

Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin. Kotila, T., Wioland, H., Enkavi, G. et al. Nat Commun (2019) 10:5320-5320. DOI 10.1038/s41467-019-13213-2 · 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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