3AAA: Actin capping protein

Crystal Structure of Actin capping protein in complex with V-1. Determined by X-ray diffraction at 2.2 Å resolution. Released 4 Aug 2010.

Method
X-ray diffraction
Resolution
2.2 Å
Organisms
Gallus gallus, Homo sapiens
Chains
3
Atoms
5,396
Mol. weight
77.85 kDa
Ligands
IPA
Released
4 Aug 2010

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

Secondary structure: helices and β-sheets

3AAA contains 35 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: 13 helices, 11 β-strands

ElementResiduesLengthSheet
α-helix10-2213
α-helix24-252
α-helix29-4012
α-helix43-497
α-helix52-609
β-strand63-6531
α-helix66-672
β-strand74-7631
α-helix78-803
β-strand81-8332
β-strand86-8942
β-strand94-9962
β-strand104-11072
α-helix118-13518
β-strand139-148103
β-strand151-164143
α-helix165-1673
β-strand169-182143
β-strand185-198143
β-strand203-217153
α-helix221-24929
α-helix250-2545
α-helix255-2584
α-helix271-2744
Chain B: 13 helices, 10 β-strands
ElementResiduesLengthSheet
α-helix3-1513
α-helix18-203
α-helix21-299
α-helix33-353
α-helix36-427
α-helix46-483
β-strand49-5134
β-strand58-6034
α-helix63-653
β-strand66-6725
β-strand70-7235
β-strand79-8025
α-helix91-11222
β-strand116-12493
β-strand127-138123
β-strand144-159163
α-helix160-1623
β-strand164-181183
β-strand185-202183
α-helix209-23022
α-helix231-2355
α-helix236-2438
α-helix248-2503
Chain C: 9 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix3-119
α-helix15-239
α-helix31-322
α-helix38-447
α-helix48-558
α-helix71-788
α-helix81-899
α-helix104-1074
α-helix111-1177

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
F-actin-capping protein subunit alpha-1Aprotein286Gallus gallusP13127 (AlphaFold model)
F-actin-capping protein subunit beta isoforms 1 and 2Bprotein277Gallus gallusP14315 (AlphaFold model)
MyotrophinCprotein123Homo sapiensP58546 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3AAA_1 F-actin-capping protein subunit alpha-1 (chains A)
MADFEDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMD
QFTPVKIEGYDDQVLITEHGDLGNGRFLDPRNKISFKFDHLRKEASDPQPEDTESALKQW
RDACDSALRAYVKDHYPNGFCTVYGKSIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFT
ITPPTAQVAAVLKIQVHYYEDGNVQLVSHKDIQDSVQVSSDVQTAKEFIKIIENAENEYQ
TAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA
Sequence of entity 2 (B), FASTA
>3AAA_2 F-actin-capping protein subunit beta isoforms 1 and 2 (chains B)
MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYL
LCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVY
LWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTN
KTGSGTMNLGGSLTRQMEKDETVSDSSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIV
NGLRSIDAIPDNQKYKQLQRELSQVLTQRQIYIQPDN
Sequence of entity 3 (C), FASTA
>3AAA_3 Myotrophin (chains C)
GPLGSMCDKEFMWALKNGDLDEVKDYVAKGEDVNRTLEGGRKPLHYAADCGQLEILEFLL
LKGADINAPDKHHITPLLSAVYEGHVSCVKLLLSKGADKTVKGPDGLTAFEATDNQAIKA
LLQ

Ligands and cofactors

IDNameFormulaCopies
IPAIsopropyl alcoholC3 H8 O2

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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