Structure of human Smoothened in complex with cholesterol and SAG. Determined by X-ray diffraction at 3.0 Å resolution. Released 15 Jun 2022.
Explore 7ZI0 in 3D Show helices and sheets RCSB PDB PDBe
7ZI0 contains 62 α-helices and 31 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 |
|---|---|---|---|
| α-helix | 59-61 | 3 | |
| α-helix | 62-64 | 3 | |
| β-strand | 65-67 | 3 | 1 |
| β-strand | 71-72 | 2 | 2 |
| β-strand | 77-78 | 2 | 3 |
| β-strand | 81-82 | 2 | 3 |
| β-strand | 87-88 | 2 | 2 |
| α-helix | 99-109 | 11 | |
| α-helix | 110-113 | 4 | |
| α-helix | 116-130 | 15 | |
| β-strand | 134-135 | 2 | 1 |
| β-strand | 138-140 | 3 | 1 |
| α-helix | 141-143 | 3 | |
| α-helix | 144-151 | 8 | |
| α-helix | 155-160 | 6 | |
| α-helix | 165-167 | 3 | |
| β-strand | 197-199 | 3 | 4 |
| α-helix | 203-205 | 3 | |
| β-strand | 213-215 | 3 | 4 |
| β-strand | 216 | 1 | 5 |
| α-helix | 224-254 | 31 | |
| α-helix | 256-259 | 4 | |
| α-helix | 264-282 | 19 | |
| α-helix | 283-285 | 3 | |
| α-helix | 289-294 | 6 | |
| β-strand | 295 | 1 | 6 |
| β-strand | 300 | 1 | 5 |
| β-strand | 301 | 1 | 6 |
| α-helix | 302 | 1 | |
| β-strand | 305 | 1 | 7 |
| α-helix | 313-342 | 30 | |
| α-helix | 344-346 | 3 | |
| α-helix | 357-378 | 22 | |
| β-strand | 381-384 | 4 | 7 |
| β-strand | 389-392 | 4 | 7 |
| α-helix | 397-400 | 4 | |
| α-helix | 401-405 | 5 | |
| α-helix | 406-452 | 47 | |
| α-helix | 456-475 | 20 | |
| α-helix | 489-514 | 26 | |
| α-helix | 517-530 | 14 | |
| α-helix | 531-536 | 6 | |
| α-helix | 537-547 | 11 | |
| α-helix | 551-599 | 49 | |
| α-helix | 607-610 | 4 | |
| α-helix | 619-637 | 19 | |
| α-helix | 638-640 | 3 | |
| α-helix | 643-656 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 59-61 | 3 | |
| β-strand | 65-67 | 3 | 8 |
| β-strand | 71-72 | 2 | 9 |
| β-strand | 77-78 | 2 | 10 |
| β-strand | 81-82 | 2 | 10 |
| β-strand | 87-88 | 2 | 9 |
| α-helix | 99-109 | 11 | |
| α-helix | 110-113 | 4 | |
| α-helix | 116-130 | 15 | |
| β-strand | 134 | 1 | 8 |
| β-strand | 138-140 | 3 | 8 |
| α-helix | 141-143 | 3 | |
| α-helix | 144-151 | 8 | |
| α-helix | 155-160 | 6 | |
| α-helix | 165-167 | 3 | |
| α-helix | 189-191 | 3 | |
| α-helix | 193-194 | 2 | |
| β-strand | 197-199 | 3 | 11 |
| β-strand | 213-215 | 3 | 11 |
| β-strand | 216 | 1 | 12 |
| α-helix | 224-254 | 31 | |
| α-helix | 256-259 | 4 | |
| α-helix | 264-282 | 19 | |
| α-helix | 283-285 | 3 | |
| α-helix | 289-294 | 6 | |
| β-strand | 295 | 1 | 13 |
| β-strand | 300 | 1 | 12 |
| β-strand | 301 | 1 | 13 |
| α-helix | 302 | 1 | |
| α-helix | 313-342 | 30 | |
| α-helix | 357-378 | 22 | |
| β-strand | 381-384 | 4 | 14 |
| β-strand | 389-392 | 4 | 14 |
| α-helix | 397-400 | 4 | |
| α-helix | 401-405 | 5 | |
| α-helix | 406-452 | 47 | |
| α-helix | 456-475 | 20 | |
| α-helix | 489-514 | 26 | |
| α-helix | 517-530 | 14 | |
| α-helix | 531-536 | 6 | |
| α-helix | 537-547 | 11 | |
| α-helix | 551-594 | 44 | |
| α-helix | 619-637 | 19 | |
| α-helix | 638-640 | 3 | |
| α-helix | 643-654 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Smoothened homolog,Soluble cytochrome b562 | A, B | protein | 638 | Homo sapiens | P0ABE7 (AlphaFold model), Q99835 (AlphaFold model) |
>7ZI0_1 Smoothened homolog,Soluble cytochrome b562 (chains A, B) SSGNATGPGPRSAGGSARRSAAVTGPPPPLSHCGRAAPCEPLRYNVCLGSVLPYGATSTL LAGDSDSQEEAHGKLVLWSGLRNAPRCWAVIQPLLCAVYMPKCENDRVELPSRTLCQATR GPCAIVERERGWPDFLRCTPDRFPEGCTNEVQNIKFNSSGQCEVPLVRTDNPKSWYEDVE GCGIQCQNPLFTEAEHQDMHSYIAAFGAVTGLCTLFTLATFVADWRNSNRYPAVILFYVN ACFFVGSIGWLAQFMDGARREIVCRADGTMRLGEPTSNETLSCVIIFVIVYYALMAGFVW FVVLTYAWHTSFKALGTTYQPLSGKTSYFHLLTWSLPFVLTVAILAVAQVDGDSVSGICF VGYKNYRYRAGFVLAPIGLVLIVGGYFLIRGVMTLFSARRQLADLEDNWETLNDNLKVIE KADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKL ANEGKVKEAQAAAEQLKTTRNAYIQKYLERARSTLSKINETMLRLGIFGFLAFGFVLITF SCHFYDFFNQAEWERSFRDYVLCQANVTIGLPTKQPIPDCEIKNRPSLLVEKINLFAMFG TGIAMSTWVWTKATLLIWRRTWCRLTGQGTETSQVAPA
| ID | Name | Formula | Copies |
|---|---|---|---|
| V0S | 3-chloro-N-[trans-4-(methylamino)cyclohexyl]-N-{[3-(pyridin-4-yl)phenyl]methyl}… | C28 H28 Cl N3 O S | 2 |
| CLR | Cholesterol | C27 H46 O | 2 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 1 |
| MPG | [(Z)-octadec-9-enyl] (2R)-2,3-bis(oxidanyl)propanoate | C21 H40 O4 | 1 |
Water and common crystallization additives (NA) are not listed.
Patched 1 regulates Smoothened by controlling sterol binding to its extracellular cysteine-rich domain. Kinnebrew, M., Woolley, R.E., Ansell, T.B. et al. Sci Adv (2022) 8:eabm5563-eabm5563. DOI 10.1126/sciadv.abm5563 · PubMed
Other PDB entries of the same protein (UniProt P0ABE7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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