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.
Explore 8GT4 in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-12 | 5 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 24 | 1 | 2 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35-38 | 4 | 3 |
| β-strand | 53-54 | 2 | 3 |
| α-helix | 55-60 | 6 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-68 | 4 | 3 |
| β-strand | 71-72 | 2 | 4 |
| β-strand | 75-76 | 2 | 4 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-94 | 7 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 1 |
| β-strand | 112 | 1 | 5 |
| α-helix | 113-121 | 9 | |
| α-helix | 122-126 | 5 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 6 |
| β-strand | 160-166 | 7 | 6 |
| β-strand | 169-170 | 2 | 6 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 6 |
| α-helix | 182-194 | 13 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 7 |
| α-helix | 246 | 1 | |
| β-strand | 247-250 | 4 | 7 |
| α-helix | 253-259 | 7 | |
| α-helix | 264-267 | 4 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-294 | 8 | |
| β-strand | 297-300 | 4 | 6 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 6 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-346 | 9 | |
| α-helix | 350-353 | 4 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-369 | 3 | |
| α-helix | 370-373 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12 | 1 | 5 |
| α-helix | 20-30 | 11 | |
| α-helix | 34-36 | 3 | |
| β-strand | 44-51 | 8 | 8 |
| β-strand | 54-57 | 4 | 8 |
| α-helix | 58-59 | 2 | |
| α-helix | 60-62 | 3 | |
| β-strand | 65-67 | 3 | 9 |
| β-strand | 71-78 | 8 | 8 |
| β-strand | 88-95 | 8 | 8 |
| α-helix | 101-117 | 17 | |
| α-helix | 122 | 1 | |
| β-strand | 123-128 | 6 | 8 |
| α-helix | 134-137 | 4 | |
| β-strand | 146-148 | 3 | 9 |
| α-helix | 152-154 | 3 | |
| α-helix | 156 | 1 | |
| β-strand | 157 | 1 | 2 |
| α-helix | 158 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha cardiac muscle 1 | A | protein | 391 | Homo sapiens | P68032 (AlphaFold model) |
| Actin-binding protein fragmin P | B | protein | 160 | Physarum polycephalum | Q94707 (AlphaFold model) |
>8GT4_1 Actin, alpha cardiac muscle 1 (chains A) MGWSHPQFEKGGIEGRDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVM VGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTL LTEAPLNPKANREKMTQIMFETFNVPAMYVAIAAVLSLYASGRTTGIVLDSGDGVTHNVP IYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFE NEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMK CDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGS ILASLSTFQQMWISKQEYDEAGPSIVHRKCF
>8GT4_2 Actin-binding protein fragmin P (chains B) MQKQKEYNIADSNIANLGTELEKKVKLEASQHEDAWKGAGKQVGVEIWRIQQFKVVPVPK KHHGSFYTGDSYIVLSTYHPKTNPDKLAYDVHFWLGAFTTQDEAGTAAYKTVELDDYLGG LPVQYREVQGYESERFLSLFPKGGLRILDGGVETGFHHVE
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 2 |
| PO4 | Phosphate ion | O4 P | 2 |
| MG | Magnesium ion | Mg | 1 |
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 1 |
Water and common crystallization additives (EDO) are not listed.
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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