9W33: S5A1-bound inactive SSTR5 structure

S5A1-bound inactive SSTR5 structure. Determined by electron microscopy at 2.69 Å resolution. Released 21 Jan 2026.

Method: Electron microscopy
Resolution: 2.69 Å
Organisms: Homo sapiens, Escherichia coli
Chains: 2
Atoms: 6,072
Mol. weight: 86.29 kDa
Ligands: A1EVQ
Released: 21 Jan 2026

Explore 9W33 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9W33 contains 35 α-helices and 4 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.

Chain A: 18 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	42-67	26
α-helix	69-71	3
α-helix	74-90	17
α-helix	93-102	10
α-helix	108-141	34
α-helix	146-149	4
α-helix	153-170	18
α-helix	174-177	4
β-strand	179-180	2	1
β-strand	186-187	2	1
α-helix	193-194	2
α-helix	196-206	11
α-helix	207-211	5
α-helix	212-1022	41
α-helix	1028-1048	21
α-helix	1059-1071	13
α-helix	1093-1097	5
α-helix	1105-273	41
α-helix	280-307	28
α-helix	309-316	8

Chain B: 17 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	39-67	29
α-helix	69-71	3
α-helix	74-90	17
α-helix	93-102	10
α-helix	109-142	34
α-helix	153-171	19
α-helix	174-177	4
β-strand	179-180	2	2
β-strand	186-187	2	2
α-helix	196-206	11
α-helix	207-211	5
α-helix	212-1022	41
α-helix	1028-1048	21
α-helix	1059-1069	11
α-helix	1073-1080	8
α-helix	1090-1095	6
α-helix	1102-273	44
α-helix	280-307	28
α-helix	309-317	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Somatostatin receptor type 5,Soluble cytochrome b562	A, B	protein	389	Homo sapiens, Escherichia coli	P0ABE7 (AlphaFold model), P35346 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9W33_1 Somatostatin receptor type 5,Soluble cytochrome b562 (chains A, B)
SAGARAVLVPVLYLLVCAAGLGGNTLVIYVVLRFAKMKTVTNIYILNLAVADVLYMLGLP
FLATQNAASFWPFGPVLCRLVMTLDGVNQFTSVFCLTVMSVDRYLAVVHPLSSARWRRPR
VAKLASAAAWVLSLCMSLPLLVFADVQEGGTCNASWPEPVGLWGAVFIIYTAVLGFFAPL
LVICLCYLLIVVKVRAARRQLADLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALD
AQKGGSGGRSPEMKDFRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYIQKY
LERARSTLRSERKVTRMVLVVVLVFAGCWLPFFTVNIVNLAVALPQEPASAGLYFFVVIL
SYANSCANPVLYGFLSDNFRQSFQKVLCL

Ligands and cofactors

ID	Name	Formula	Copies
A1EVQ	4-[8-[(2-cyclopropyl-5-ethoxy-4-methyl-phenyl)methyl]-2-oxidanylidene-1,3,8-tri…	C27 H33 N3 O4	2

Primary citation

Structural insights into nonpeptide antagonist inhibition of somatostatin receptor subtype 5. Li, Y., Xing, Z., Hu, W. et al. Proc Natl Acad Sci U S A (2025) 122:e2522515122-e2522515122. DOI 10.1073/pnas.2522515122 · 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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