3AA6: Actin capping protein

Crystal structure of Actin capping protein in complex with the Cp-binding motif derived from CD2AP. Determined by X-ray diffraction at 1.9 Å resolution. Released 4 Aug 2010.

Method
X-ray diffraction
Resolution
1.9 Å
Organisms
Gallus gallus, homo sapiens
Chains
3
Atoms
4,829
Mol. weight
63.23 kDa
Ligands
BA
Released
4 Aug 2010

Explore 3AA6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3AA6 contains 25 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: 11 helices, 11 β-strands

ElementResiduesLengthSheet
α-helix10-2213
α-helix24-252
α-helix29-4012
α-helix43-6018
β-strand64-6631
β-strand73-7531
α-helix78-803
β-strand8112
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-helix221-24929
α-helix250-2556
α-helix256-2583
α-helix271-2755
Chain B: 11 helices, 10 β-strands
ElementResiduesLengthSheet
α-helix5-139
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
α-helix141-1433
β-strand145-158143
β-strand164-181183
β-strand185-202183
α-helix209-23022
α-helix231-2366
α-helix237-2437
Chain C: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix489-4924
α-helix499-5024
α-helix503-5053

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)
23mer peptide from CD2-associated proteinCprotein23homo sapiensQ9Y5K6 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3AA6_1 F-actin-capping protein subunit alpha-1 (chains A)
MADFEDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMD
QFTPVKIEGYDDQVLITEHGDLGNGRFLDPRNKISFKFDHLRKEASDPQPEDTESALKQW
RDACDSALRAYVKDHYPNGFCTVYGKSIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFT
ITPPTAQVAAVLKIQVHYYEDGNVQLVSHKDIQDSVQVSSDVQTAKEFIKIIENAENEYQ
TAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA
Sequence of entity 2 (B), FASTA
>3AA6_2 F-actin-capping protein subunit beta isoforms 1 and 2 (chains B)
MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYL
LCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVY
LWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTN
KTGSGTMNLGGSLTRQMEKDETVSDSSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIV
NGLR
Sequence of entity 3 (C), FASTA
>3AA6_3 23mer peptide from CD2-associated protein (chains C)
NLLHLTANRPKMPGRRLPGRFNG

Ligands and cofactors

IDNameFormulaCopies
BABarium ionBa1

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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