8GSU: Human cardiac alpha actin

Crystal structure of human cardiac alpha actin (WT_ADP-Pi) in complex with fragmin F1 domain. Determined by X-ray diffraction at 1.5 Å resolution. Released 8 Mar 2023.

Method
X-ray diffraction
Resolution
1.5 Å
Organisms
Homo sapiens, Physarum polycephalum
Chains
2
Atoms
5,212
Mol. weight
62.9 kDa
Ligands
CA, MG, PO4, ADP
Released
8 Mar 2023

Explore 8GSU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8GSU contains 38 α-helices and 30 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: 27 helices, 21 β-strands

ElementResiduesLengthSheet
β-strand8-1251
β-strand16-2161
β-strand2412
β-strand29-3241
β-strand35-3843
β-strand53-5423
α-helix55-606
α-helix62-643
β-strand65-6843
β-strand71-7224
β-strand75-7624
α-helix79-879
α-helix88-947
α-helix98-1003
β-strand103-10751
β-strand11215
α-helix113-1219
α-helix122-1265
β-strand131-13661
α-helix137-1448
β-strand150-15566
β-strand160-16676
β-strand169-17026
α-helix172-1743
β-strand176-17836
α-helix182-19211
α-helix193-1964
α-helix203-21614
α-helix223-23210
β-strand238-24147
β-strand247-25047
α-helix253-2597
α-helix264-2674
α-helix271-2733
α-helix274-28310
α-helix287-2893
α-helix290-2945
β-strand297-30046
α-helix302-3043
α-helix309-32012
β-strand329-33026
α-helix335-3373
α-helix338-3469
α-helix350-3545
β-strand357-35821
α-helix359-3657
α-helix367-3693
α-helix370-3734
Chain B: 11 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix9-113
β-strand1215
α-helix20-3011
α-helix34-363
β-strand44-5188
β-strand54-5748
α-helix58-592
α-helix60-623
β-strand65-6739
β-strand71-7888
β-strand88-9588
α-helix101-11717
α-helix1221
β-strand123-12868
α-helix134-1374
β-strand146-14839
α-helix152-1543
α-helix1561
β-strand15712
α-helix158-1592

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin, alpha cardiac muscle 1Aprotein391Homo sapiensP68032 (AlphaFold model)
Actin-binding protein fragmin PBprotein162Physarum polycephalumQ94707 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8GSU_1 Actin, alpha cardiac muscle 1 (chains A)
MGWSHPQFEKGGIEGRDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVM
VGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTL
LTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVP
IYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFE
NEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMK
CDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGS
ILASLSTFQQMWISKQEYDEAGPSIVHRKCF
Sequence of entity 2 (B), FASTA
>8GSU_2 Actin-binding protein fragmin P (chains B)
GPMQKQKEYNIADSNIANLGTELEKKVKLEASQHEDAWKGAGKQVGVEIWRIQQFKVVPV
PKKHHGSFYTGDSYIVLSTYHPKTNPDKLAYDVHFWLGAFTTQDEAGTAAYKTVELDDYL
GGLPVQYREVQGYESERFLSLFPKGGLRILDGGVETGFHHVE

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa2
MGMagnesium ionMg1
PO4Phosphate ionO4 P3
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P21

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

Primary citation

Mutagenic analysis of actin reveals the mechanism of His161 flipping that triggers ATP hydrolysis. Iwasa, M., Takeda, S., Narita, A. et al. Front Cell Dev Biol (2023) 11:1105460-1105460. DOI 10.3389/fcell.2023.1105460 · PubMed

Other PDB entries of the same protein (UniProt P68032 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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