9W32: Antagonist 1-bound inactive SSTR5 structure

antagonist 1-bound inactive SSTR5 structure. Determined by electron microscopy at 2.59 Å resolution. Released 21 Jan 2026.

Method: Electron microscopy
Resolution: 2.59 Å
Organisms: Homo sapiens, Escherichia coli
Chains: 2
Atoms: 6,078
Mol. weight: 86.38 kDa
Ligands: A1EVP
Released: 21 Jan 2026

Explore 9W32 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9W32 contains 37 α-helices and 2 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, 0 β-strands

Element	Residues	Length
α-helix	42-67	26
α-helix	69-71	3
α-helix	74-90	17
α-helix	93-102	10
α-helix	108-142	35
α-helix	146-150	5
α-helix	153-171	19
α-helix	174-177	4
α-helix	196-206	11
α-helix	207-211	5
α-helix	212-1022	41
α-helix	1028-1046	19
α-helix	1055-1080	26
α-helix	1090-1096	7
α-helix	1097-1102	6
α-helix	1103-273	43
α-helix	280-307	28
α-helix	309-315	7

Chain B: 19 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	108-142	35
α-helix	148-150	3
α-helix	153-171	19
α-helix	174-177	4
α-helix	196-206	11
α-helix	207-211	5
α-helix	212-1022	41
α-helix	1028-1046	19
α-helix	1047-1051	5
α-helix	1055-1078	24
α-helix	1090-1096	7
α-helix	1097-1102	6
α-helix	1103-273	43
α-helix	280-307	28
α-helix	309-315	7
β-strand	316	1	1
β-strand	319	1	1

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

>9W32_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
A1EVP	1-[2-[[3,5-diethoxy-4-(4-fluorophenyl)phenyl]methyl]-5-oxa-2,6-diazaspiro[3.4]o…	C28 H34 F N3 O5	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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