Crystal structure of human cardiac alpha actin A108G mutant (ADP-Pi state) in complex with fragmin F1 domain. Determined by X-ray diffraction at 1.35 Å resolution. Released 8 Mar 2023.
Explore 8GT1 in 3D Show helices and sheets RCSB PDB PDBe
8GT1 contains 36 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 |
|---|---|---|---|
| α-helix | 6-7 | 2 | |
| 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 | 56-60 | 5 | |
| 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 | 113-125 | 13 | |
| 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 | 287-294 | 8 | |
| β-strand | 297-300 | 4 | 6 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 6 |
| α-helix | 335-337 | 3 | |
| 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) |
>8GT1_1 Actin, alpha cardiac muscle 1 (chains A) MGWSHPQFEKGGIEGRDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVM VGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTL LTEGPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVP IYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFE NEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMK CDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGS ILASLSTFQQMWISKQEYDEAGPSIVHRKCF
>8GT1_2 Actin-binding protein fragmin P (chains B) GPMQKQKEYNIADSNIANLGTELEKKVKLEASQHEDAWKGAGKQVGVEIWRIQQFKVVPV PKKHHGSFYTGDSYIVLSTYHPKTNPDKLAYDVHFWLGAFTTQDEAGTAAYKTVELDDYL GGLPVQYREVQGYESERFLSLFPKGGLRILDGGVETGFHHVE
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 1 |
| PO4 | Phosphate ion | O4 P | 3 |
| MG | Magnesium ion | Mg | 1 |
| CA | Calcium ion | Ca | 2 |
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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