Complex of ATP-actin With the C-terminal Actin-Binding Domain of Tropomodulin. Determined by X-ray diffraction at 2.3 Å resolution. Released 30 Jul 2014.
Explore 4PKI in 3D Show helices and sheets RCSB PDB PDBe
4PKI contains 38 α-helices and 33 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 | 22 | 1 | 2 |
| β-strand | 24 | 1 | 2 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35-38 | 4 | 3 |
| α-helix | 45-47 | 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 | 88-93 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 5 |
| β-strand | 160-166 | 7 | 5 |
| β-strand | 169-170 | 2 | 5 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 5 |
| α-helix | 182-194 | 13 | |
| α-helix | 206-216 | 11 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 6 |
| β-strand | 247-250 | 4 | 6 |
| α-helix | 253-262 | 10 | |
| α-helix | 264-267 | 4 | |
| α-helix | 272-273 | 2 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-289 | 3 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 5 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 5 |
| α-helix | 338-348 | 11 | |
| 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 | 57-61 | 5 | |
| β-strand | 67-74 | 8 | 7 |
| β-strand | 77-80 | 4 | 7 |
| α-helix | 81-82 | 2 | |
| α-helix | 83-85 | 3 | |
| β-strand | 88-90 | 3 | 8 |
| β-strand | 94-102 | 9 | 7 |
| α-helix | 107 | 1 | |
| β-strand | 108-116 | 9 | 7 |
| α-helix | 122-138 | 17 | |
| β-strand | 144-149 | 6 | 7 |
| α-helix | 155-158 | 4 | |
| β-strand | 166-168 | 3 | 8 |
| α-helix | 172-174 | 3 | |
| α-helix | 1177-1178 | 2 | |
| α-helix | 1183-1191 | 9 | |
| β-strand | 1199-1201 | 3 | 9 |
| α-helix | 1210-1220 | 11 | |
| β-strand | 1228-1230 | 3 | 9 |
| α-helix | 1238-1248 | 11 | |
| β-strand | 1256-1258 | 3 | 9 |
| α-helix | 1266-1274 | 9 | |
| α-helix | 1276-1278 | 3 | |
| β-strand | 1284-1286 | 3 | 9 |
| α-helix | 1296-1306 | 11 | |
| β-strand | 1314-1316 | 3 | 9 |
| α-helix | 1322-1345 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha skeletal muscle | A | protein | 377 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
| Gelsolin,Tropomodulin-1 chimera | G | protein | 324 | Homo sapiens | P06396 (AlphaFold model), P28289 (AlphaFold model) |
>4PKI_1 Actin, alpha skeletal muscle (chains A) MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT KQEYDEAGPSIVHRKCF
>4PKI_2 Gelsolin,Tropomodulin-1 chimera (chains G) MVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYD LHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGG VASGFGGSGGSGGSGLNSVIKPTQYKPVPDEEPNSTDVEETLERIKNNDPKLEEVNLNNI RNIPIPTLKAYAEALKENSYVKKFSIVGTRSNDPVAYALAEMLKENKVLKTLNVESNFIS GAGILRLVEALPYNTSLVEMKIDNQSQPLGNKVEMEIVSMLEKNATLLKFGYHFTQQGPR LRASNAMMNNNDLVRKRRLADLTG
Actin cytoskeleton. Mechanism of actin filament pointed-end capping by tropomodulin. Rao, J.N., Madasu, Y., Dominguez, R. Science (2014) 345:463-467. DOI 10.1126/science.1256159 · PubMed
Other PDB entries of the same protein (UniProt P68135 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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