Revised model of leiomodin 2-mediated actin regulation (alternate refinement of PDB 4RWT). Determined by X-ray diffraction at 3.0 Å resolution. Released 30 Aug 2017.
Explore 5WFN in 3D Show helices and sheets RCSB PDB PDBe
5WFN contains 60 α-helices and 52 β-strands across 4 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 | 17-21 | 5 | 1 |
| β-strand | 24 | 1 | 2 |
| β-strand | 29-31 | 3 | 1 |
| β-strand | 35-38 | 4 | 3 |
| β-strand | 53-54 | 2 | 3 |
| α-helix | 56-59 | 4 | |
| 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 | 113-121 | 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 |
| β-strand | 176-178 | 3 | 5 |
| α-helix | 182-196 | 15 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 6 |
| β-strand | 247-250 | 4 | 6 |
| α-helix | 252-262 | 11 | |
| α-helix | 264-267 | 4 | |
| α-helix | 274-283 | 10 | |
| 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 | |
| α-helix | 350-352 | 3 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-370 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 199-208 | 10 | |
| β-strand | 215-217 | 3 | 7 |
| α-helix | 226-237 | 12 | |
| β-strand | 244-246 | 3 | 7 |
| α-helix | 254-266 | 13 | |
| β-strand | 272-274 | 3 | 7 |
| α-helix | 282-291 | 10 | |
| α-helix | 292-294 | 3 | |
| β-strand | 300-302 | 3 | 7 |
| α-helix | 312-322 | 11 | |
| β-strand | 330-332 | 3 | 7 |
| α-helix | 338-363 | 26 | |
| α-helix | 520-530 | 11 | |
| α-helix | 534-536 | 3 | |
| β-strand | 538 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin-5C | A, B | protein | 384 | Drosophila melanogaster | P10987 (AlphaFold model) |
| Leiomodin-2 | C, D | protein | 506 | Homo sapiens | Q6P5Q4 (AlphaFold model) |
>5WFN_1 Actin-5C (chains A, B) MCDEEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ SKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKM TQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLD LAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKS YELPDGQVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIREDLYANTVL SGGTTMYPGIADRMQKEITALAKSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISK QEYDESGPSIVHRKCFASHHHHHH
>5WFN_2 Leiomodin-2 (chains C, D) MAHHHHHHVGTMSTFGYRRGLSKYESIDEDELLASLSAEELKELERELEDIEPDRNLPVG LRQKSLTEKTPTGTFSREALMAYWEKESQKLLEKERLGECGKVAEDKEEEEDSDEEERTI ETAKGINGTVNYDSVNSDNSKPKIFKSQIENINLTNGSNGRNTESPAAIHPCGNPTVIED ALDKIKSNDPDTTEVNLNNIENITTQTLTRFAEALKDNTVVKTFSLANTHADDSAAMAIA EMLKVNEHITNVNVESNFITGKGILAIMRALQHNTVLTELRFHNQRHIMGSQVEMEIVKL LKENTTLLRLGYHFELPGPRMSMTSILTRNMDKQRQKRLQEQKQQEGYDGGPNLRTKVWQ RGTPSSSPYVSPRHSPWSSPKLPKKVQTVRSRPLSPVATPPPPPPPPLPEKKLITRNIAE VIKQQESAQRALQNGQGSGSGGSVGSQPNSILKEIKNSLRSVQEKKMEDSSRPSTPQRSA HENLMEAIRGSSIKQLKRVEVPEALR
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 2 |
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 2 |
Crystal structure of leiomodin 2 in complex with actin: a structural and functional reexamination. Boczkowska, M., Yurtsever, Z., Rebowski, G. et al. Biophys J (2017) 113:889-899. DOI 10.1016/j.bpj.2017.07.007
Other PDB entries of the same protein (UniProt P10987 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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