Actin complex with Gelsolin Segment 1 fused to Cobl segment. Determined by X-ray diffraction at 3.0 Å resolution. Released 26 Sept 2012.
Explore 3TU5 in 3D Show helices and sheets RCSB PDB PDBe
3TU5 contains 32 α-helices and 28 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 | 56-60 | 5 | |
| 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 |
| 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 | 182-195 | 14 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-231 | 9 | |
| β-strand | 238-241 | 4 | 6 |
| β-strand | 247-250 | 4 | 6 |
| α-helix | 253-259 | 7 | |
| 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 | 5 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 5 |
| α-helix | 338-346 | 9 | |
| α-helix | 350-355 | 6 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-372 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-10 | 5 | |
| β-strand | 16-23 | 8 | 7 |
| β-strand | 26-29 | 4 | 7 |
| α-helix | 30-31 | 2 | |
| α-helix | 32-34 | 3 | |
| β-strand | 37-39 | 3 | 8 |
| β-strand | 43-51 | 9 | 7 |
| β-strand | 57-65 | 9 | 7 |
| α-helix | 71-87 | 17 | |
| α-helix | 92 | 1 | |
| β-strand | 93-98 | 6 | 7 |
| α-helix | 104-107 | 4 | |
| β-strand | 115-117 | 3 | 8 |
| α-helix | 121-123 | 3 | |
| α-helix | 125 | 1 | |
| β-strand | 126 | 1 | 2 |
| α-helix | 127 | 1 | |
| α-helix | 129-131 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha skeletal muscle | A | protein | 377 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
| Gelsolin,Protein cordon-bleu,Thymosin beta-4 | B | protein | 297 | Homo sapiens, Mus musculus | P06396 (AlphaFold model), P62328 (AlphaFold model), Q5NBX1 (AlphaFold model) |
>3TU5_1 Actin, alpha skeletal muscle (chains A) MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT KQEYDEAGPSIVHRKCF
>3TU5_2 Gelsolin,Protein cordon-bleu,Thymosin beta-4 (chains B) MNHKVHHHHHHIEGRHMGSVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGD AYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFE SATFLGYFKSGLKYKKGGVASKLRKVAEQTSEGRPKKPSYVEAESERSALLAAIRGHSGT LSLRKVSSLASEELQSFRNAALGAPGLDKPQQEDLGLPPPPALPPPPAPAPQAPSASVTV SRFSTGTPSNSVNARQALMDAIRSGTGAARLRKTETQEKNPLPSKETIEQEKQAGES
Water and common crystallization additives (MPD) are not listed.
Structural States and dynamics of the d-loop in actin. Durer, Z.A., Kudryashov, D.S., Sawaya, M.R. et al. Biophys J (2012) 103:930-939. DOI 10.1016/j.bpj.2012.07.030 · 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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