8WM9: Fzd4/DEP complex

Fzd4/DEP complex. Determined by electron microscopy at 3.53 Å resolution. Released 11 Sept 2024.

Method
Electron microscopy
Resolution
3.53 Å
Organism
Homo sapiens
Chains
3
Atoms
5,879
Mol. weight
204 kDa
Ligands
Y01
Released
11 Sept 2024

Explore 8WM9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 16 helices, 6 β-strands

ElementResiduesLengthSheet
β-strand191-19331
β-strand200-20231
β-strand20312
α-helix2041
α-helix213-24331
α-helix253-27523
α-helix277-2804
β-strand29112
α-helix296-2983
α-helix300-33132
α-helix341-3433
α-helix344-36522
β-strand369-37023
β-strand377-37823
α-helix384-3863
α-helix387-3926
α-helix393-42028
α-helix428-46033
α-helix462-4643
α-helix472-48918
α-helix493-4953
α-helix498-51013
Chain B: 16 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix213-24331
α-helix245-2473
α-helix254-27522
α-helix277-2804
β-strand28214
β-strand29214
α-helix300-3067
α-helix307-3115
α-helix312-33120
α-helix337-3415
α-helix344-36522
β-strand368-37035
β-strand377-37935
α-helix384-3874
α-helix388-3925
α-helix393-41725
α-helix433-46028
α-helix462-4676
α-helix472-48918
α-helix498-51215
Chain C: 3 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix423-4308
β-strand440-44456
β-strand447-45266
β-strand453-45427
α-helix455-46410
α-helix475-48410
β-strand48918
β-strand502-50327
β-strand50418

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Frizzled-4A, Bprotein537Homo sapiensQ9ULV1 (AlphaFold model)
Segment polarity protein dishevelled homolog DVL-2Cprotein736Homo sapiensO14641 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>8WM9_1 Frizzled-4 (chains A, B)
MAWRGAGPSVPGAPGGVGLSLGLLLQLLLLLGPARGFGDEEERRCDPIRISMCQNLGYNV
TKMPNLVGHELQTDAELQLTTFTPLIQYGCSSQLQFFLCSVYVPMCTEKINIPIGPCGGM
CLSVKRRCEPVLKEFGFAWPESLNCSKFPPQNDHNHMCMEGPGDEEVPLPHKTPIQPGEE
CHSVGTNSDQYIWVKRSLNCVLKCGYDAGLYSRSAKEFTDIWMAVWASLCFISTAFTVLT
FLIDSSRFSYPERPIIFLSMCYNIYSIAYIVRLTVGRERISCDFEEAAEPVLIQEGLKNT
GCAIIFLLLYFFGMASSIWWVILTLTWFLAAGLKWGHEAIEMHSSYFHIAAWAIPAVKTI
VILIMRLVDADELTGLCYVGNQNLDALTGFVVAPLFTYLVIGTLFIAAGLVALFKIRSNL
QKDGTKTDKLERLMVKIGVFSVLYTVPATIVIACYFYEISNWALFRYSADDSNMAVEMLK
IFMSLLVGITSGMWIWSAKTLHTWQKFYNRLVNSGKVKREKRGNGWVKPGKGSETVV
Sequence of entity 2 (C), FASTA
>8WM9_2 Segment polarity protein dishevelled homolog DVL-2 (chains C)
MAGSSTGGGGVGETKVIYHLDEEETPYLVKIPVPAERITLGDFKSVLQRPAGAKYFFKSM
DQDFGVVKEEISDDNARLPCFNGRVVSWLVSSDNPQPEMAPPVHEPRAELAPPAPPLPPL
PPERTSGIGDSRPPSFHPNVSSSHENLEPETETESVVSLRRERPRRRDSSEHGAGGHRTG
GPSRLERHLAGYESSSTLMTSELESTSLGDSDEEDTMSRFSSSTEQSSASRLLKRHRRRR
KQRPPRLERTSSFSSVTDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIM
KGGAVAADGRIEPGDMLLQVNDMNFENMSNDDAVRVLRDIVHKPGPIVLTVAKCWDPSPQ
AYFTLPRNEPIQPIDPAAWVSHSAALTGTFPAYPGSSSMSTITSGSSLPDGCEGRGLSVH
TDMASVTKAMAAPESGLEVRDRMWLKITIPNAFLGSDVVDWLYHHVEGFPERREARKYAS
GLLKAGLIRHTVNKITFSEQCYYVFGDLSGGCESYLVNLSLNDNDGSSGASDQDTLAPLP
GATPWPLLPTFSYQYPAPHPYSPQPPPYHELSSYTYGGGSASSQHSEGSRSSGSTRSDGG
AGRTGRPEERAPESKSGSGSESEPSSRGGSLRRGGEASGTSDGGPPPSRGSTGGAPNLRA
HPGLHPYGPPPGMALPYNPMMVVMMPPPPPPVPPAVQPPGAPPVRDLGSVPPELTASRQS
FHMAMGNPSEFFVDVM

Ligands and cofactors

IDNameFormulaCopies
Y01Cholesterol hemisuccinateC31 H50 O410

Primary citation

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:

Browse structure collections

About this viewer

MolViewer shows 8WM9 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.