Crystal structure of human cardiac alpha actin Q137A mutant (ADP-Pi state) in complex with fragmin F1 domain. Determined by X-ray diffraction at 1.4 Å resolution. Released 8 Mar 2023.
Explore 8GT5 in 3D Show helices and sheets RCSB PDB PDBe
8GT5 contains 37 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 | 182-193 | 12 | |
| α-helix | 194-196 | 3 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 7 |
| β-strand | 247-250 | 4 | 7 |
| α-helix | 253-262 | 10 | |
| α-helix | 264-267 | 4 | |
| α-helix | 271-273 | 3 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-289 | 3 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 6 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 6 |
| α-helix | 338-346 | 9 | |
| α-helix | 350-354 | 5 | |
| 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 |
|---|---|---|---|
| α-helix | 9-11 | 3 | |
| 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 | 158-159 | 2 |
| 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 | 162 | Physarum polycephalum | Q94707 (AlphaFold model) |
>8GT5_1 Actin, alpha cardiac muscle 1 (chains A) MGWSHPQFEKGGIEGRDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVM VGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTL LTEAPLNPKANREKMTQIMFETFNVPAMYVAIAAVLSLYASGRTTGIVLDSGDGVTHNVP IYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFE NEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMK CDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGS ILASLSTFQQMWISKQEYDEAGPSIVHRKCF
>8GT5_2 Actin-binding protein fragmin P (chains B) GPMQKQKEYNIADSNIANLGTELEKKVKLEASQHEDAWKGAGKQVGVEIWRIQQFKVVPV PKKHHGSFYTGDSYIVLSTYHPKTNPDKLAYDVHFWLGAFTTQDEAGTAAYKTVELDDYL GGLPVQYREVQGYESERFLSLFPKGGLRILDGGVETGFHHVE
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 2 |
| PO4 | Phosphate ion | O4 P | 3 |
| MG | Magnesium ion | Mg | 1 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 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:
MolViewer shows 8GT5 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.