Structure of Komagataella pastoris actin-thymosin beta4 hybrid. Determined by X-ray diffraction at 2.3 Å resolution. Released 22 Oct 2014.
Explore 4PL7 in 3D Show helices and sheets RCSB PDB PDBe
4PL7 contains 57 α-helices and 44 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 | 1 | 3 |
| β-strand | 54 | 1 | 3 |
| α-helix | 56-59 | 4 | |
| β-strand | 68 | 1 | 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 | 113-121 | 9 | |
| α-helix | 122-126 | 5 | |
| 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 | 223-230 | 8 | |
| β-strand | 238-241 | 4 | 6 |
| β-strand | 247-250 | 4 | 6 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-261 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 274-282 | 9 | |
| α-helix | 287-294 | 8 | |
| β-strand | 297-300 | 4 | 5 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 5 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-347 | 10 | |
| α-helix | 350-355 | 6 | |
| α-helix | 356 | 1 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-364 | 6 | |
| α-helix | 395-400 | 6 | |
| α-helix | 403-405 | 3 | |
| β-strand | 407 | 1 | 2 |
| α-helix | 408 | 1 | |
| β-strand | 412-413 | 2 | 1 |
| α-helix | 416-419 | 4 | |
| α-helix | 420-427 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-12 | 5 | 7 |
| β-strand | 16-21 | 6 | 7 |
| β-strand | 24 | 1 | 8 |
| β-strand | 29-32 | 4 | 7 |
| β-strand | 35 | 1 | 9 |
| β-strand | 54 | 1 | 9 |
| α-helix | 56-59 | 4 | |
| β-strand | 68 | 1 | 9 |
| β-strand | 71-72 | 2 | 10 |
| β-strand | 75-76 | 2 | 10 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-94 | 7 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 7 |
| α-helix | 113-121 | 9 | |
| α-helix | 122-126 | 5 | |
| β-strand | 131-136 | 6 | 7 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 11 |
| β-strand | 160-166 | 7 | 11 |
| β-strand | 169-170 | 2 | 11 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 11 |
| α-helix | 182-194 | 13 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-230 | 8 | |
| β-strand | 238-241 | 4 | 12 |
| β-strand | 247-250 | 4 | 12 |
| α-helix | 253-256 | 4 | |
| α-helix | 258-261 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 274-282 | 9 | |
| α-helix | 287-294 | 8 | |
| β-strand | 297-300 | 4 | 11 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-320 | 12 | |
| α-helix | 326-327 | 2 | |
| β-strand | 329-330 | 2 | 11 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-347 | 10 | |
| α-helix | 353-355 | 3 | |
| α-helix | 356 | 1 | |
| β-strand | 357-358 | 2 | 7 |
| α-helix | 359-363 | 5 | |
| α-helix | 395-400 | 6 | |
| α-helix | 403-405 | 3 | |
| β-strand | 407 | 1 | 8 |
| α-helix | 408 | 1 | |
| β-strand | 412-413 | 2 | 7 |
| α-helix | 416-419 | 4 | |
| α-helix | 420-427 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin,Thymosin beta-4 | A, B | protein | 440 | Komagataella pastoris, Homo sapiens | P62328 (AlphaFold model), Q9P4D1 (AlphaFold model) |
>4PL7_1 Actin,Thymosin beta-4 (chains A, B) DGEDVAALVIDNGSGMCKAGYAGDDAPHTVFPSVVGRPRHQGVMVGMGQKDSFVGDEAQS KRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRLAPEEHPVLLTEAPMNPKSNREKMT QIMFETFNVPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYAGFSLPHAILRIDL AGRDLTDYLMKILSERGYTFSTSAEREIVRDIKEKLCYVALDFDQELQTSSQSSSIEKSY ELPDGQVITIGNERFRAPEALFHPSVLGLEASGIDQTTYNSIMKCDVDVRKELYSNIVMS GGTTMFPGIAERMQKELTALAPSSMKVKISAPPERKYSVWIGGSILASLGTFQQMWISKQ EYDESGPSIVHLKCFASRGGSGGSSGGSASDKPDMAEIEKFDKSKLKKTETQEKNPLPSK ETIEQEKQAGESGTLEVLFQ
Structural basis of thymosin-beta 4/profilin exchange leading to actin filament polymerization. Xue, B., Leyrat, C., Grimes, J.M. et al. Proc Natl Acad Sci U S A (2014) 111:E4596-E4605. DOI 10.1073/pnas.1412271111 · PubMed
Other PDB entries of the same protein (UniProt P62328 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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