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- PDB-9vqo: The structure of DmOR67d-DmOrco in the apo state -

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Basic information

Entry
Database: PDB / ID: 9vqo
TitleThe structure of DmOR67d-DmOrco in the apo state
Components
  • Odorant receptor 67d
  • Odorant receptor coreceptor
KeywordsMEMBRANE PROTEIN / Odorant Receptor / Complex / channel
Function / homology
Function and homology information


detection of pheromone / ionotropic olfactory receptor activity / sensory dendrite / olfactory receptor activity / response to pheromone / courtship behavior / detection of chemical stimulus involved in sensory perception of smell / olfactory behavior / odorant binding / cation channel complex ...detection of pheromone / ionotropic olfactory receptor activity / sensory dendrite / olfactory receptor activity / response to pheromone / courtship behavior / detection of chemical stimulus involved in sensory perception of smell / olfactory behavior / odorant binding / cation channel complex / behavioral response to ethanol / intracellularly gated calcium channel activity / coreceptor activity / dendrite membrane / sensory perception of smell / regulation of protein localization / calmodulin binding / cilium / dendrite / signal transduction / protein homodimerization activity / plasma membrane
Similarity search - Function
Olfactory receptor, insect / 7tm Odorant receptor
Similarity search - Domain/homology
Odorant receptor coreceptor / Odorant receptor 67d
Similarity search - Component
Biological speciesDrosophila melanogaster (fruit fly)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsWang, J. / Guo, J.
Funding support China, 1items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2020YFA0908501 China
CitationJournal: Cell Res. / Year: 2026
Title: Cryo-EM structures of Drosophila OR67d-Orco complexes reveal insect pheromone sensing mechanism.
Authors: Wang, J. / Yang, C. / Chang, S. / Jiao, D. / Lin, J. / Yang, X. / Cai, W. / Ma, D. / Ding, Z.J. / Huang, J. / Huang, J. / Fan, M. / Hu, M. / Wang, Y. / Xu, H. / Su, N. / Guo, J.
History
DepositionJul 5, 2025Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Jul 1, 2026Provider: repository / Type: Initial release
Revision 1.0Jul 1, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Jul 1, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jul 1, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jul 1, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Jul 1, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Odorant receptor 67d
B: Odorant receptor coreceptor
C: Odorant receptor coreceptor
D: Odorant receptor coreceptor


Theoretical massNumber of molelcules
Total (without water)205,2924
Polymers205,2924
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Odorant receptor 67d


Mass: 43936.207 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: Or67d, CG14157 / Production host: Homo sapiens (human) / References: UniProt: Q9VT92
#2: Protein Odorant receptor coreceptor / Odorant receptor 83b


Mass: 53785.227 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: Orco, A45, Or83b, CG10609 / Production host: Homo sapiens (human) / References: UniProt: Q9VNB5
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: The structure of DmOR67d-DmOrco in the apo state / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Drosophila melanogaster (fruit fly)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 1600 nm / Nominal defocus min: 800 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K2 QUANTUM (4k x 4k)

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Processing

EM software
IDNameVersionCategory
1RELION3.1particle selection
13RELION3.13D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 234510 / Symmetry type: POINT

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