3AA0: Actin Capping Protein

Crystal structure of Actin Capping Protein in complex with the Cp-binding motif derived from CARMIL. Determined by X-ray diffraction at 1.7 Å resolution. Released 4 Aug 2010.

Method
X-ray diffraction
Resolution
1.7 Å
Organisms
Gallus gallus, mus musculus
Chains
3
Atoms
4,836
Mol. weight
63.15 kDa
Ligands
CO3
Released
4 Aug 2010

Explore 3AA0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3AA0 contains 24 α-helices and 21 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: 12 helices, 11 β-strands

ElementResiduesLengthSheet
α-helix10-2213
α-helix24-252
α-helix29-4012
α-helix43-497
α-helix51-6010
β-strand64-6521
β-strand74-7521
α-helix78-803
β-strand81-8332
β-strand86-8942
β-strand94-9962
β-strand104-11072
α-helix118-13518
β-strand140-14893
β-strand151-164143
α-helix165-1673
β-strand169-182143
β-strand185-198143
β-strand202-217163
α-helix221-25030
α-helix251-2555
α-helix256-2583
α-helix271-2744
Chain B: 10 helices, 10 β-strands
ElementResiduesLengthSheet
α-helix3-1311
α-helix18-203
α-helix21-3111
α-helix33-353
α-helix36-427
β-strand48-5254
β-strand57-6154
α-helix63-653
β-strand66-6725
β-strand70-7235
β-strand79-8025
α-helix91-11222
β-strand116-12493
β-strand127-137113
β-strand144-158153
β-strand164-181183
β-strand185-202183
α-helix209-23022
α-helix231-2355
α-helix236-2438
Chain C: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix989-9924
α-helix994-9952

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
F-actin-capping protein subunit alpha-1Aprotein286Gallus gallusP13127 (AlphaFold model)
F-actin-capping protein subunit beta isoforms 1 and 2Bprotein244Gallus gallusP14315 (AlphaFold model)
21mer peptide from Leucine-rich repeat-containing protein 16ACprotein21mus musculusQ6EDY6 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3AA0_1 F-actin-capping protein subunit alpha-1 (chains A)
MADFEDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMD
QFTPVKIEGYDDQVLITEHGDLGNGRFLDPRNKISFKFDHLRKEASDPQPEDTESALKQW
RDACDSALRAYVKDHYPNGFCTVYGKSIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFT
ITPPTAQVAAVLKIQVHYYEDGNVQLVSHKDIQDSVQVSSDVQTAKEFIKIIENAENEYQ
TAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA
Sequence of entity 2 (B), FASTA
>3AA0_2 F-actin-capping protein subunit beta isoforms 1 and 2 (chains B)
MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYL
LCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVY
LWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTN
KTGSGTMNLGGSLTRQMEKDETVSDSSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIV
NGLR
Sequence of entity 3 (C), FASTA
>3AA0_3 21mer peptide from Leucine-rich repeat-containing protein 16A (chains C)
RLEHFTKLRPKRNKKQQPTQA

Ligands and cofactors

IDNameFormulaCopies
CO3Carbonate ionC O31

Primary citation

Two distinct mechanisms for actin capping protein regulation--steric and allosteric inhibition. Takeda, S., Minakata, S., Koike, R. et al. PLoS Biol (2010) 8:e1000416-e1000416. DOI 10.1371/journal.pbio.1000416 · PubMed

Other PDB entries of the same protein (UniProt P13127 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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