Fzd4/DEP complex. Determined by electron microscopy at 3.53 Å resolution. Released 11 Sept 2024.
Explore 8WM9 in 3D Show helices and sheets RCSB PDB PDBe
8WM9 contains 35 α-helices and 16 β-strands across 3 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 | 191-193 | 3 | 1 |
| β-strand | 200-202 | 3 | 1 |
| β-strand | 203 | 1 | 2 |
| α-helix | 204 | 1 | |
| α-helix | 213-243 | 31 | |
| α-helix | 253-275 | 23 | |
| α-helix | 277-280 | 4 | |
| β-strand | 291 | 1 | 2 |
| α-helix | 296-298 | 3 | |
| α-helix | 300-331 | 32 | |
| α-helix | 341-343 | 3 | |
| α-helix | 344-365 | 22 | |
| β-strand | 369-370 | 2 | 3 |
| β-strand | 377-378 | 2 | 3 |
| α-helix | 384-386 | 3 | |
| α-helix | 387-392 | 6 | |
| α-helix | 393-420 | 28 | |
| α-helix | 428-460 | 33 | |
| α-helix | 462-464 | 3 | |
| α-helix | 472-489 | 18 | |
| α-helix | 493-495 | 3 | |
| α-helix | 498-510 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 213-243 | 31 | |
| α-helix | 245-247 | 3 | |
| α-helix | 254-275 | 22 | |
| α-helix | 277-280 | 4 | |
| β-strand | 282 | 1 | 4 |
| β-strand | 292 | 1 | 4 |
| α-helix | 300-306 | 7 | |
| α-helix | 307-311 | 5 | |
| α-helix | 312-331 | 20 | |
| α-helix | 337-341 | 5 | |
| α-helix | 344-365 | 22 | |
| β-strand | 368-370 | 3 | 5 |
| β-strand | 377-379 | 3 | 5 |
| α-helix | 384-387 | 4 | |
| α-helix | 388-392 | 5 | |
| α-helix | 393-417 | 25 | |
| α-helix | 433-460 | 28 | |
| α-helix | 462-467 | 6 | |
| α-helix | 472-489 | 18 | |
| α-helix | 498-512 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 423-430 | 8 | |
| β-strand | 440-444 | 5 | 6 |
| β-strand | 447-452 | 6 | 6 |
| β-strand | 453-454 | 2 | 7 |
| α-helix | 455-464 | 10 | |
| α-helix | 475-484 | 10 | |
| β-strand | 489 | 1 | 8 |
| β-strand | 502-503 | 2 | 7 |
| β-strand | 504 | 1 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Frizzled-4 | A, B | protein | 537 | Homo sapiens | Q9ULV1 (AlphaFold model) |
| Segment polarity protein dishevelled homolog DVL-2 | C | protein | 736 | Homo sapiens | O14641 (AlphaFold model) |
>8WM9_1 Frizzled-4 (chains A, B) MAWRGAGPSVPGAPGGVGLSLGLLLQLLLLLGPARGFGDEEERRCDPIRISMCQNLGYNV TKMPNLVGHELQTDAELQLTTFTPLIQYGCSSQLQFFLCSVYVPMCTEKINIPIGPCGGM CLSVKRRCEPVLKEFGFAWPESLNCSKFPPQNDHNHMCMEGPGDEEVPLPHKTPIQPGEE CHSVGTNSDQYIWVKRSLNCVLKCGYDAGLYSRSAKEFTDIWMAVWASLCFISTAFTVLT FLIDSSRFSYPERPIIFLSMCYNIYSIAYIVRLTVGRERISCDFEEAAEPVLIQEGLKNT GCAIIFLLLYFFGMASSIWWVILTLTWFLAAGLKWGHEAIEMHSSYFHIAAWAIPAVKTI VILIMRLVDADELTGLCYVGNQNLDALTGFVVAPLFTYLVIGTLFIAAGLVALFKIRSNL QKDGTKTDKLERLMVKIGVFSVLYTVPATIVIACYFYEISNWALFRYSADDSNMAVEMLK IFMSLLVGITSGMWIWSAKTLHTWQKFYNRLVNSGKVKREKRGNGWVKPGKGSETVV
>8WM9_2 Segment polarity protein dishevelled homolog DVL-2 (chains C) MAGSSTGGGGVGETKVIYHLDEEETPYLVKIPVPAERITLGDFKSVLQRPAGAKYFFKSM DQDFGVVKEEISDDNARLPCFNGRVVSWLVSSDNPQPEMAPPVHEPRAELAPPAPPLPPL PPERTSGIGDSRPPSFHPNVSSSHENLEPETETESVVSLRRERPRRRDSSEHGAGGHRTG GPSRLERHLAGYESSSTLMTSELESTSLGDSDEEDTMSRFSSSTEQSSASRLLKRHRRRR KQRPPRLERTSSFSSVTDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIM KGGAVAADGRIEPGDMLLQVNDMNFENMSNDDAVRVLRDIVHKPGPIVLTVAKCWDPSPQ AYFTLPRNEPIQPIDPAAWVSHSAALTGTFPAYPGSSSMSTITSGSSLPDGCEGRGLSVH TDMASVTKAMAAPESGLEVRDRMWLKITIPNAFLGSDVVDWLYHHVEGFPERREARKYAS GLLKAGLIRHTVNKITFSEQCYYVFGDLSGGCESYLVNLSLNDNDGSSGASDQDTLAPLP GATPWPLLPTFSYQYPAPHPYSPQPPPYHELSSYTYGGGSASSQHSEGSRSSGSTRSDGG AGRTGRPEERAPESKSGSGSESEPSSRGGSLRRGGEASGTSDGGPPPSRGSTGGAPNLRA HPGLHPYGPPPGMALPYNPMMVVMMPPPPPPVPPAVQPPGAPPVRDLGSVPPELTASRQS FHMAMGNPSEFFVDVM
| ID | Name | Formula | Copies |
|---|---|---|---|
| Y01 | Cholesterol hemisuccinate | C31 H50 O4 | 10 |
Structural basis of Frizzled 4 in recognition of Dishevelled 2 unveils mechanism of WNT signaling activation. Qian, Y., Ma, Z., Xu, Z. et al. Nat Commun (2024) 15:7644-7644. DOI 10.1038/s41467-024-52174-z · PubMed
Other PDB entries of the same protein (UniProt Q9ULV1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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