8GT4: Human cardiac alpha actin Q137A mutant

Crystal structure of human cardiac alpha actin Q137A mutant (AMPPNP state) in complex with fragmin F1 domain. Determined by X-ray diffraction at 1.55 Å resolution. Released 8 Mar 2023.

Method
X-ray diffraction
Resolution
1.55 Å
Organisms
Homo sapiens, Physarum polycephalum
Chains
2
Atoms
4,990
Mol. weight
62.61 kDa
Ligands
CA, PO4, MG, ANP
Released
8 Mar 2023

Explore 8GT4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8GT4 contains 35 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: 25 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-helix182-19413
α-helix203-21614
α-helix223-23210
β-strand238-24147
α-helix2461
β-strand247-25047
α-helix253-2597
α-helix264-2674
α-helix274-28310
α-helix287-2948
β-strand297-30046
α-helix302-3043
α-helix309-32012
β-strand329-33026
α-helix335-3373
α-helix338-3469
α-helix350-3534
β-strand357-35821
α-helix359-3657
α-helix367-3693
α-helix370-3734
Chain B: 10 helices, 9 β-strands
ElementResiduesLengthSheet
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-helix1581

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin, alpha cardiac muscle 1Aprotein391Homo sapiensP68032 (AlphaFold model)
Actin-binding protein fragmin PBprotein160Physarum polycephalumQ94707 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8GT4_1 Actin, alpha cardiac muscle 1 (chains A)
MGWSHPQFEKGGIEGRDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVM
VGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTL
LTEAPLNPKANREKMTQIMFETFNVPAMYVAIAAVLSLYASGRTTGIVLDSGDGVTHNVP
IYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFE
NEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMK
CDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGS
ILASLSTFQQMWISKQEYDEAGPSIVHRKCF
Sequence of entity 2 (B), FASTA
>8GT4_2 Actin-binding protein fragmin P (chains B)
MQKQKEYNIADSNIANLGTELEKKVKLEASQHEDAWKGAGKQVGVEIWRIQQFKVVPVPK
KHHGSFYTGDSYIVLSTYHPKTNPDKLAYDVHFWLGAFTTQDEAGTAAYKTVELDDYLGG
LPVQYREVQGYESERFLSLFPKGGLRILDGGVETGFHHVE

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa2
PO4Phosphate ionO4 P2
MGMagnesium ionMg1
ANPPhosphoaminophosphonic acid-adenylate esterC10 H17 N6 O12 P31

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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