4QIN: Human smoothened receptor

Structure of the human smoothened receptor in complex with SAG1.5. Determined by X-ray diffraction at 2.6 Å resolution. Released 23 Jul 2014.

Method: X-ray diffraction
Resolution: 2.6 Å
Organisms: Homo sapiens, Escherichia coli
Chains: 1
Atoms: 3,454
Mol. weight: 52.92 kDa
Ligands: SG8
Released: 23 Jul 2014

Explore 4QIN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4QIN contains 21 α-helices and 9 β-strands across 1 chain. 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: 21 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	197-199	3	1
α-helix	207	1
β-strand	213-215	3	1
β-strand	216	1	2
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	3
β-strand	300	1	2
β-strand	301	1	3
β-strand	305	1	4
α-helix	313-344	32
α-helix	353-377	25
β-strand	381-384	4	4
β-strand	389-392	4	4
α-helix	399-400	2
α-helix	401-405	5
α-helix	406-1018	46
α-helix	1023-1041	19
α-helix	1046-1048	3
α-helix	1056-1079	24
α-helix	1084-1101	18
α-helix	1103-1106	4
α-helix	444-446	3
α-helix	447-490	44
α-helix	515-533	19
α-helix	534-536	3
α-helix	539-544	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Smoothened homolog/Soluble cytochrome b562 chimeric protein	A	protein	468	Homo sapiens, Escherichia coli	P0ABE7 (AlphaFold model), Q99835 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4QIN_1 Smoothened homolog/Soluble cytochrome b562 chimeric protein (chains A)
GGTSGQCEVPLVRTDNPKSWYEDVEGCGIQCQNPLFTEAEHQDMHSYIAAFGAVTGLCTL
FTLATFVADWRNSNRYPAVILFYVNACFFVGSIGWLAQFMDGARREIVCRADGTMRLGEP
TSNETLSCVIIFVIVYYALMAGVVWFVVLTYAWHTSFKALGTTYQPLSGKTSYFHLLTWS
LPFVLTVAILAVAQVDGDSVSGICFVGYKNYRYRAGFVLAPIGLVLIVGGYFLIRGVMTL
FSIKSNHADLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSP
DSPEMKDFRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYIQKYLAASKINE
TMLRLGIFGFLAFGFVLITFSCHFYDFFNQAEWERSFRDYVLCQANVTIGLPTKQPIPDC
EIKNRPSLLVEKINLFAMFGTGIAMSTWVWTKATLLIWRRTWCRLTGQ

Ligands and cofactors

ID	Name	Formula	Copies
SG8	3-chloro-4,7-difluoro-N-[trans-4-(methylamino)cyclohexyl]-N-[3-(pyridin-4-yl)be…	C28 H26 Cl F2 N3 O S	1

Primary citation

Structural basis for Smoothened receptor modulation and chemoresistance to anticancer drugs. Wang, C., Wu, H., Evron, T. et al. Nat Commun (2014) 5:4355-4355. DOI 10.1038/ncomms5355 · PubMed

Other PDB entries of the same protein (UniProt P0ABE7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6DYF 1.1 Å, Cu(II)-bound structure of the engineered cyt cb562 variant, CH3Y
5YO6 1.2 Å, Crystal Structure of B562RIL with engineered disulfide bond T9C-A36C
4JEA 1.22 Å, Crystal structure of an engineered Zn-RIDC1 construct with four interfacial disulfide…
7LSJ 1.26 Å, Cu-bound crystal structure of the engineered cyt cb562 variant, DiCyt2 - H63A,…
7MK4 1.27 Å, Co-bound crystal structure of the engineered cyt cb562 variant, DiCyt2
6DYC 1.33 Å, Co(II)-bound structure of the engineered cyt cb562 variant, CH3
5YO4 1.37 Å, Crystal Structure of B562RIL with engineered disulfide bond K27C-A79C
256B 1.4 Å, Improvement of the 2.5 Å resolution model of cytochrome B562 by redetermining the…
6OT4 1.4 Å, Bimetallic dodecameric cage design 2 (BMC2) from cytochrome cb562
7LRV 1.4 Å, Ni-bound crystal structure of the engineered cyt cb562 variant, DiCyt2, crystallized in…
9PQ4 1.48 Å, Bi-bound structure of the H77C variant of TriCyt2
6DYG 1.49 Å, Fe(II)-bound structure of the engineered cyt cb562 variant, CH3Y

Browse structure collections

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