Structure of actin-Lmod complex. Determined by X-ray diffraction at 2.98 Å resolution. Released 14 Oct 2015.
Explore 4RWT in 3D Show helices and sheets RCSB PDB PDBe
4RWT contains 67 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 | 8-11 | 4 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35-38 | 4 | 2 |
| α-helix | 44-46 | 3 | |
| 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 | 79-87 | 9 | |
| α-helix | 88-93 | 6 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 113-121 | 9 | |
| α-helix | 122-126 | 5 | |
| β-strand | 131 | 1 | 4 |
| β-strand | 132-136 | 5 | 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 | 182-195 | 14 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 6 |
| β-strand | 247-250 | 4 | 6 |
| α-helix | 253-256 | 4 | |
| α-helix | 259-262 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 272-273 | 2 | |
| 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 | 350-355 | 6 | |
| β-strand | 358 | 1 | 4 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-369 | 3 | |
| α-helix | 370-373 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-11 | 4 | 10 |
| β-strand | 16-21 | 6 | 10 |
| β-strand | 24 | 1 | 9 |
| β-strand | 29-32 | 4 | 10 |
| β-strand | 35-38 | 4 | 11 |
| β-strand | 53-54 | 2 | 11 |
| α-helix | 56-60 | 5 | |
| β-strand | 65-68 | 4 | 11 |
| β-strand | 71-72 | 2 | 12 |
| β-strand | 75-76 | 2 | 12 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-93 | 6 | |
| β-strand | 103-107 | 5 | 10 |
| α-helix | 113-121 | 9 | |
| α-helix | 122-126 | 5 | |
| β-strand | 131 | 1 | 13 |
| β-strand | 132-136 | 5 | 10 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 14 |
| β-strand | 160-166 | 7 | 14 |
| β-strand | 169-170 | 2 | 14 |
| β-strand | 176-178 | 3 | 14 |
| α-helix | 182-195 | 14 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 15 |
| β-strand | 247-250 | 4 | 15 |
| α-helix | 253-256 | 4 | |
| α-helix | 259-262 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 272-273 | 2 | |
| α-helix | 274-283 | 10 | |
| α-helix | 290-294 | 5 | |
| β-strand | 297-300 | 4 | 14 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 14 |
| α-helix | 338-348 | 11 | |
| α-helix | 350-355 | 6 | |
| β-strand | 358 | 1 | 13 |
| α-helix | 359-365 | 7 | |
| α-helix | 367-370 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 167-176 | 10 | |
| β-strand | 183-185 | 3 | 7 |
| α-helix | 194-203 | 10 | |
| β-strand | 212-216 | 5 | 7 |
| α-helix | 222-232 | 11 | |
| β-strand | 240-244 | 5 | 7 |
| α-helix | 250-259 | 10 | |
| α-helix | 260-262 | 3 | |
| β-strand | 268-270 | 3 | 7 |
| α-helix | 281-289 | 9 | |
| α-helix | 290-292 | 3 | |
| β-strand | 298-300 | 3 | 7 |
| α-helix | 306-330 | 25 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 167-176 | 10 | |
| β-strand | 183-185 | 3 | 8 |
| α-helix | 195-203 | 9 | |
| β-strand | 212-214 | 3 | 8 |
| α-helix | 222-233 | 12 | |
| β-strand | 240-242 | 3 | 8 |
| α-helix | 250-259 | 10 | |
| α-helix | 260-262 | 3 | |
| β-strand | 268-270 | 3 | 8 |
| α-helix | 281-289 | 9 | |
| α-helix | 290-292 | 3 | |
| β-strand | 298-300 | 3 | 8 |
| α-helix | 306-327 | 22 | |
| α-helix | 328-332 | 5 | |
| α-helix | 408-416 | 9 | |
| α-helix | 438-441 | 4 | |
| α-helix | 443-445 | 3 | |
| α-helix | 468-478 | 11 | |
| α-helix | 482-484 | 3 | |
| β-strand | 486 | 1 | 9 |
| α-helix | 487 | 1 |
| 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) |
>4RWT_1 Actin-5C (chains A, B) MCDEEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ SKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKM TQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLD LAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKS YELPDGQVITIGNERFRCPEALFQPSFLGMEACGIHETTYNSIMKCDVDIREDLYANTVL SGGTTMYPGIADRMQKEITALAKSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISK QEYDESGPSIVHRKCFASHHHHHH
>4RWT_2 Leiomodin-2 (chains C, D) MAHHHHHHVGTMSTFGYRRGLSKYESIDEDELLASLSAEELKELERELEDIEPDRNLPVG LRQKSLTEKTPTGTFSREALMAYWEKESQKLLEKERLGECGKVAEDKEEEEDSDEEERTI ETAKGINGTVNYDSVNSDNSKPKIFKSQIENINLTNGSNGRNTESPAAIHPCGNPTVIED ALDKIKSNDPDTTEVNLNNIENITTQTLTRFAEALKDNTVVKTFSLANTHADDSAAMAIA EMLKVNEHITNVNVESNFITGKGILAIMRALQHNTVLTELRFHNQRHIMGSQVEMEIVKL LKENTTLLRLGYHFELPGPRMSMTSILTRNMDKQRQKRLQEQKQQEGYDGGPNLRTKVWQ RGTPSSSPYVSPRHSPWSSPKLPKKVQTVRSRPLSPVATPPPPPPPPLPEKKLITRNIAE VIKQQESAQRALQNGQGSGSGGSVGSQPNSILKEIKNSLRSVQEKKMEDSSRPSTPQRSA HENLMEAIRGSSIKQLKRVEVPEALR
| ID | Name | Formula | Copies |
|---|---|---|---|
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 2 |
| MG | Magnesium ion | Mg | 2 |
Mechanisms of leiomodin 2-mediated regulation of actin filament in muscle cells. Chen, X., Ni, F., Kondrashkina, E. et al. Proc Natl Acad Sci U S A (2015) 112:12687-12692. DOI 10.1073/pnas.1512464112 · PubMed
Other PDB entries of the same protein (UniProt P10987 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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