Crystal structure of fragmin domain-1 in complex with actin (AMPPNP-form). Determined by X-ray diffraction at 1.15 Å resolution. Released 26 Oct 2022.
Explore 7W4Z in 3D Show helices and sheets RCSB PDB PDBe
7W4Z 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 | 113-125 | 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 | 274-283 | 10 | |
| α-helix | 287-289 | 3 | |
| α-helix | 290-294 | 5 | |
| 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 | 369-373 | 5 |
| 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 skeletal muscle | A | protein | 377 | Gallus gallus | P68139 (AlphaFold model) |
| Actin-binding protein fragmin P | B | protein | 162 | Physarum polycephalum | Q94707 (AlphaFold model) |
>7W4Z_1 Actin, alpha skeletal muscle (chains A) MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT KQEYDEAGPSIVHRKCF
>7W4Z_2 Actin-binding protein fragmin P (chains B) GPMQKQKEYNIADSNIANLGTELEKKVKLEASQHEDAWKGAGKQVGVEIWRIQQFKVVPV PKKHHGSFYTGDSYIVLSTYHPKTNPDKLAYDVHFWLGAFTTQDEAGTAAYKTVELDDYL GGLPVQYREVQGYESERFLSLFPKGGLRILDGGVETGFHHVE
| ID | Name | Formula | Copies |
|---|---|---|---|
| PO4 | Phosphate ion | O4 P | 2 |
| CA | Calcium ion | Ca | 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.
Structures and mechanisms of actin ATP hydrolysis. Kanematsu, Y., Narita, A., Oda, T. et al. Proc Natl Acad Sci U S A (2022) 119:e2122641119-e2122641119. DOI 10.1073/pnas.2122641119 · PubMed
Other PDB entries of the same protein (UniProt P68139 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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