Profilin:actin with a wide open nucleotide cleft. Determined by X-ray diffraction at 2.2 Å resolution. Released 25 Apr 2012.
Explore 3UB5 in 3D Show helices and sheets RCSB PDB PDBe
3UB5 contains 28 α-helices and 26 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 | 30-32 | 3 | 1 |
| β-strand | 35-38 | 4 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 56-60 | 5 | |
| β-strand | 65-68 | 4 | 2 |
| β-strand | 71-72 | 2 | 3 |
| β-strand | 75-76 | 2 | 3 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-93 | 5 | |
| 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 | 4 |
| β-strand | 160-166 | 7 | 4 |
| β-strand | 169-170 | 2 | 4 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 4 |
| α-helix | 182-196 | 15 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-231 | 9 | |
| β-strand | 238-241 | 4 | 5 |
| β-strand | 247-250 | 4 | 5 |
| α-helix | 253-256 | 4 | |
| α-helix | 259-262 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 274-282 | 9 | |
| α-helix | 287-294 | 8 | |
| β-strand | 297-300 | 4 | 4 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 4 |
| α-helix | 338-347 | 10 | |
| 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 | 4-11 | 8 | |
| β-strand | 16-23 | 8 | 6 |
| β-strand | 29-33 | 5 | 6 |
| α-helix | 39-41 | 3 | |
| α-helix | 44-51 | 8 | |
| α-helix | 57-61 | 5 | |
| β-strand | 63-65 | 3 | 6 |
| β-strand | 68-75 | 8 | 6 |
| β-strand | 84-89 | 6 | 6 |
| β-strand | 99-104 | 6 | 6 |
| β-strand | 108-114 | 7 | 6 |
| α-helix | 115 | 1 | |
| α-helix | 120-136 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, cytoplasmic 1 | A | protein | 374 | Bos taurus | P60712 (AlphaFold model) |
| Profilin-1 | P | protein | 140 | Bos taurus | P02584 (AlphaFold model) |
>3UB5_1 Actin, cytoplasmic 1 (chains A) DDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSK RGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQ IMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLA GRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYE LPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSG GTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE YDESGPSIVHRKCF
>3UB5_2 Profilin-1 (chains P) XAGWNAYIDNLMADGTCQDAAIVGYKDSPSVWAAVPGKTFVNITPAEVGILVGKDRSSFF VNGLTLGGQKCSVIRDSLLQDGEFTMDLRTKSTGGAPTFNITVTMTAKTLVLLMGKEGVH GGMINKKCYEMASHLRRSQY
Water and common crystallization additives (GOL, CL) are not listed.
Structural basis for profilin-mediated actin nucleotide exchange. Porta, J.C., Borgstahl, G.E. J Mol Biol (2012) 418:103-116. DOI 10.1016/j.jmb.2012.02.012 · PubMed
Other PDB entries of the same protein (UniProt P60712 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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