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- EMDB-23119: Orexin Receptor 2 (OX2R) in Complex with G Protein and Small-Mole... -

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Basic information

Entry
Database: EMDB / ID: EMD-23119
TitleOrexin Receptor 2 (OX2R) in Complex with G Protein and Small-Molecule Agonist Compound 1
Map data
Sample
  • Complex: Orexin Receptor 2 (OX2R) in Complex with G Protein and Small-Molecule Agonist Compound 1
    • Protein or peptide: Engineered Guanine nucleotide-binding protein subunit alpha
    • Protein or peptide: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
    • Protein or peptide: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
    • Protein or peptide: single-chain antibody Fv fragment (svFv16)
    • Protein or peptide: Hypocretin receptor type 2
    • Protein or peptide: Synthetic nanobody 51 (Sb51)
  • Ligand: 4'-methoxy-N,N-dimethyl-3'-{[3-(2-{[2-(2H-1,2,3-triazol-2-yl)benzene-1-carbonyl]amino}ethyl)phenyl]sulfamoyl}[1,1'-biphenyl]-3-carboxamide
Function / homology
Function and homology information


regulation of circadian sleep/wake cycle, wakefulness / circadian sleep/wake cycle process / orexin receptor activity / Orexin and neuropeptides FF and QRFP bind to their respective receptors / neuropeptide receptor activity / feeding behavior / locomotion / peptide hormone binding / neuropeptide signaling pathway / cellular response to hormone stimulus ...regulation of circadian sleep/wake cycle, wakefulness / circadian sleep/wake cycle process / orexin receptor activity / Orexin and neuropeptides FF and QRFP bind to their respective receptors / neuropeptide receptor activity / feeding behavior / locomotion / peptide hormone binding / neuropeptide signaling pathway / cellular response to hormone stimulus / regulation of cytosolic calcium ion concentration / peptide binding / Olfactory Signaling Pathway / Activation of the phototransduction cascade / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / Thromboxane signalling through TP receptor / G-protein activation / G protein-coupled acetylcholine receptor signaling pathway / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / Prostacyclin signalling through prostacyclin receptor / Glucagon signaling in metabolic regulation / G beta:gamma signalling through CDC42 / ADP signalling through P2Y purinoceptor 12 / G beta:gamma signalling through BTK / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / Sensory perception of sweet, bitter, and umami (glutamate) taste / photoreceptor disc membrane / Adrenaline,noradrenaline inhibits insulin secretion / Glucagon-type ligand receptors / Vasopressin regulates renal water homeostasis via Aquaporins / G alpha (z) signalling events / cellular response to catecholamine stimulus / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / ADORA2B mediated anti-inflammatory cytokines production / sensory perception of taste / ADP signalling through P2Y purinoceptor 1 / adenylate cyclase-activating dopamine receptor signaling pathway / G beta:gamma signalling through PI3Kgamma / cellular response to prostaglandin E stimulus / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / GPER1 signaling / G-protein beta-subunit binding / Inactivation, recovery and regulation of the phototransduction cascade / heterotrimeric G-protein complex / G alpha (12/13) signalling events / extracellular vesicle / signaling receptor complex adaptor activity / Thrombin signalling through proteinase activated receptors (PARs) / GTPase binding / retina development in camera-type eye / phospholipase C-activating G protein-coupled receptor signaling pathway / Ca2+ pathway / G alpha (i) signalling events / fibroblast proliferation / G alpha (s) signalling events / G alpha (q) signalling events / chemical synaptic transmission / cell population proliferation / Ras protein signal transduction / Extra-nuclear estrogen signaling / G protein-coupled receptor signaling pathway / lysosomal membrane / GTPase activity / synapse / protein-containing complex binding / signal transduction / extracellular exosome / membrane / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Orexin receptor 2 / Orexin receptor type 2 / Orexin receptor family / Serpentine type 7TM GPCR chemoreceptor Srsx / G-protein, gamma subunit / G-protein gamma subunit domain profile. / GGL domain / G-protein gamma-like domain superfamily / G-protein gamma-like domain / GGL domain ...Orexin receptor 2 / Orexin receptor type 2 / Orexin receptor family / Serpentine type 7TM GPCR chemoreceptor Srsx / G-protein, gamma subunit / G-protein gamma subunit domain profile. / GGL domain / G-protein gamma-like domain superfamily / G-protein gamma-like domain / GGL domain / G protein gamma subunit-like motifs / Guanine nucleotide-binding protein, beta subunit / G-protein, beta subunit / G-protein coupled receptors family 1 signature. / G protein-coupled receptor, rhodopsin-like / GPCR, rhodopsin-like, 7TM / G-protein coupled receptors family 1 profile. / 7 transmembrane receptor (rhodopsin family) / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
Orexin receptor type 2 / Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 / Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 / Orexin receptor type 2
Similarity search - Component
Biological speciesHomo sapiens (human) / Mus musculus (house mouse) / Lama glama (llama)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.0 Å
AuthorsHong C / Byrne NJ / Zamlynny B / Tummala S / Xiao L / Shipman JM / Partridge AT / Minnick C / Breslin MJ / Rudd MT ...Hong C / Byrne NJ / Zamlynny B / Tummala S / Xiao L / Shipman JM / Partridge AT / Minnick C / Breslin MJ / Rudd MT / Stachel SJ / Rada VL / Kern JC / Armacost KA / Hollingsworth SA / O'Brien JA / Hall DL / McDonald TP / Strickland C / Brooun A / Soisson SM / Hollenstein K
CitationJournal: Nat Commun / Year: 2021
Title: Structures of active-state orexin receptor 2 rationalize peptide and small-molecule agonist recognition and receptor activation.
Authors: Chuan Hong / Noel J Byrne / Beata Zamlynny / Srivanya Tummala / Li Xiao / Jennifer M Shipman / Andrea T Partridge / Christina Minnick / Michael J Breslin / Michael T Rudd / Shawn J Stachel / ...Authors: Chuan Hong / Noel J Byrne / Beata Zamlynny / Srivanya Tummala / Li Xiao / Jennifer M Shipman / Andrea T Partridge / Christina Minnick / Michael J Breslin / Michael T Rudd / Shawn J Stachel / Vanessa L Rada / Jeffrey C Kern / Kira A Armacost / Scott A Hollingsworth / Julie A O'Brien / Dawn L Hall / Terrence P McDonald / Corey Strickland / Alexei Brooun / Stephen M Soisson / Kaspar Hollenstein /
Abstract: Narcolepsy type 1 (NT1) is a chronic neurological disorder that impairs the brain's ability to control sleep-wake cycles. Current therapies are limited to the management of symptoms with modest ...Narcolepsy type 1 (NT1) is a chronic neurological disorder that impairs the brain's ability to control sleep-wake cycles. Current therapies are limited to the management of symptoms with modest effectiveness and substantial adverse effects. Agonists of the orexin receptor 2 (OXR) have shown promise as novel therapeutics that directly target the pathophysiology of the disease. However, identification of drug-like OXR agonists has proven difficult. Here we report cryo-electron microscopy structures of active-state OXR bound to an endogenous peptide agonist and a small-molecule agonist. The extended carboxy-terminal segment of the peptide reaches into the core of OXR to stabilize an active conformation, while the small-molecule agonist binds deep inside the orthosteric pocket, making similar key interactions. Comparison with antagonist-bound OXR suggests a molecular mechanism that rationalizes both receptor activation and inhibition. Our results enable structure-based discovery of therapeutic orexin agonists for the treatment of NT1 and other hypersomnia disorders.
History
DepositionDec 15, 2020-
Header (metadata) releaseFeb 10, 2021-
Map releaseFeb 10, 2021-
UpdateFeb 17, 2021-
Current statusFeb 17, 2021Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.1736
  • Imaged by UCSF Chimera
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  • Surface view colored by height
  • Surface level: 0.1736
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7l1v
  • Surface level: 0.1736
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_23119.png

Downloads & links

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Map

FileDownload / File: emd_23119.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 0.84 Å
Density
Contour LevelBy AUTHOR: 0.1736 / Movie #1: 0.1736
Minimum - Maximum-0.9046146 - 1.4924684
Average (Standard dev.)0.0020281882 (±0.029540526)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 251.99998 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.840.840.84
M x/y/z300300300
origin x/y/z0.0000.0000.000
length x/y/z252.000252.000252.000
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS300300300
D min/max/mean-0.9051.4920.002

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Supplemental data

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Sample components

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Entire : Orexin Receptor 2 (OX2R) in Complex with G Protein and Small-Mole...

EntireName: Orexin Receptor 2 (OX2R) in Complex with G Protein and Small-Molecule Agonist Compound 1
Components
  • Complex: Orexin Receptor 2 (OX2R) in Complex with G Protein and Small-Molecule Agonist Compound 1
    • Protein or peptide: Engineered Guanine nucleotide-binding protein subunit alpha
    • Protein or peptide: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
    • Protein or peptide: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
    • Protein or peptide: single-chain antibody Fv fragment (svFv16)
    • Protein or peptide: Hypocretin receptor type 2
    • Protein or peptide: Synthetic nanobody 51 (Sb51)
  • Ligand: 4'-methoxy-N,N-dimethyl-3'-{[3-(2-{[2-(2H-1,2,3-triazol-2-yl)benzene-1-carbonyl]amino}ethyl)phenyl]sulfamoyl}[1,1'-biphenyl]-3-carboxamide

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Supramolecule #1: Orexin Receptor 2 (OX2R) in Complex with G Protein and Small-Mole...

SupramoleculeName: Orexin Receptor 2 (OX2R) in Complex with G Protein and Small-Molecule Agonist Compound 1
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#6
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Engineered Guanine nucleotide-binding protein subunit alpha

MacromoleculeName: Engineered Guanine nucleotide-binding protein subunit alpha
type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 28.040881 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: GTLSAEDKAA VERSKMIEKQ LQKDKQVYRR TLRLLLLGAD NSGKSTIVKQ MRILHGGSGG SGGTSGIFET KFQVDKVNFH MFDVGGQRD ERRKWIQCFN DVTAIIFVVD SSDYNRLQEA LNDFKSIWNN RWLRTISVIL FLNKQDLLAE KVLAGKSKIE D YFPEFARY ...String:
GTLSAEDKAA VERSKMIEKQ LQKDKQVYRR TLRLLLLGAD NSGKSTIVKQ MRILHGGSGG SGGTSGIFET KFQVDKVNFH MFDVGGQRD ERRKWIQCFN DVTAIIFVVD SSDYNRLQEA LNDFKSIWNN RWLRTISVIL FLNKQDLLAE KVLAGKSKIE D YFPEFARY TTPEDATPEP GEDPRVTRAK YFIRKEFVDI STASGDGRHI CYPHFTCAVD TENARRIFND CKDIILQMNL RE YNLV

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Macromolecule #2: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1

MacromoleculeName: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 38.579148 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MGHHHHHHHH SELDQLRQEA EQLKNQIRDA RKACADATLS QITNNIDPVG RIQMRTRRTL RGHLAKIYAM HWGTDSRLLV SASQDGKLI IWDSYTTNKV HAIPLRSSWV MTCAYAPSGN YVACGGLDNI CSIYNLKTRE GNVRVSRELA GHTGYLSCCR F LDDNQIVT ...String:
MGHHHHHHHH SELDQLRQEA EQLKNQIRDA RKACADATLS QITNNIDPVG RIQMRTRRTL RGHLAKIYAM HWGTDSRLLV SASQDGKLI IWDSYTTNKV HAIPLRSSWV MTCAYAPSGN YVACGGLDNI CSIYNLKTRE GNVRVSRELA GHTGYLSCCR F LDDNQIVT SSGDTTCALW DIETGQQTTT FTGHTGDVMS LSLAPDTRLF VSGACDASAK LWDVREGMCR QTFTGHESDI NA ICFFPNG NAFATGSDDA TCRLFDLRAD QELMTYSHDN IICGITSVSF SKSGRLLLAG YDDFNCNVWD ALKADRAGVL AGH DNRVSC LGVTDDGMAV ATGSWDSFLK IWN

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Macromolecule #3: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2

MacromoleculeName: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 7.845078 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
MASNNTASIA QARKLVEQLK MEANIDRIKV SKAAADLMAY CEAHAKEDPL LTPVPASENP FREKKFFSAI L

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Macromolecule #4: single-chain antibody Fv fragment (svFv16)

MacromoleculeName: single-chain antibody Fv fragment (svFv16) / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 26.610615 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: GSDVQLVESG GGLVQPGGSR KLSCSASGFA FSSFGMHWVR QAPEKGLEWV AYISSGSGTI YYADTVKGRF TISRDDPKNT LFLQMTSLR SEDTAMYYCV RSIYYYGSSP FDFWGQGTTL TVSSGGGGSG GGGSGGGGSD IVMTQATSSV PVTPGESVSI S CRSSKSLL ...String:
GSDVQLVESG GGLVQPGGSR KLSCSASGFA FSSFGMHWVR QAPEKGLEWV AYISSGSGTI YYADTVKGRF TISRDDPKNT LFLQMTSLR SEDTAMYYCV RSIYYYGSSP FDFWGQGTTL TVSSGGGGSG GGGSGGGGSD IVMTQATSSV PVTPGESVSI S CRSSKSLL HSNGNTYLYW FLQRPGQSPQ LLIYRMSNLA SGVPDRFSGS GSGTAFTLTI SRLEAEDVGV YYCMQHLEYP LT FGAGTKL ELK

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Macromolecule #5: Hypocretin receptor type 2

MacromoleculeName: Hypocretin receptor type 2 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 43.470875 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: DYKDDDAMGT KLEDSPPCRN WSSASELNET QEPFLNPTDY DDEEFLRYLW REYLHPKEYE WVLIAGYIIV FVVALIGNVL VCVAVWKNH HMRTVTNYFI VNLSLADVLV TITCLPATLV VDITETWFFG QSLCKVIPYL QTVSVSVSVL TLSCIALDRW Y AICHPLMF ...String:
DYKDDDAMGT KLEDSPPCRN WSSASELNET QEPFLNPTDY DDEEFLRYLW REYLHPKEYE WVLIAGYIIV FVVALIGNVL VCVAVWKNH HMRTVTNYFI VNLSLADVLV TITCLPATLV VDITETWFFG QSLCKVIPYL QTVSVSVSVL TLSCIALDRW Y AICHPLMF KSTAKRARNS IVIIWIVSCI IMIPQAIVME CSTVFPGLAN KTTLFTVCDE RWGGEIYPKM YHICFFLVTY MA PLCLMVL AYLQIFRKLW CRQIPGTSSE IKQIRARRKT ARMLMVVLLV FAICYLPISI LNVLKRVFGM FAHTEDRETV YAW FTFSHW LVYANSAANP IIYNFLSGKF REEFKAAFSC CCLGVHHRHH HHHHHHHH

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Macromolecule #6: Synthetic nanobody 51 (Sb51)

MacromoleculeName: Synthetic nanobody 51 (Sb51) / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Lama glama (llama)
Molecular weightTheoretical: 12.786225 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
GSSSQVQLVE SGGGLVQAGG SLRLSCAASG FPVGRVMYWY RQAPGKEREW VAAISSHGDM TAYADSVKGR FTISRDNAKN TVYLQMNSL KPEDTAVYYC EVYVGYFYHG QGTQVTVSA

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Macromolecule #7: 4'-methoxy-N,N-dimethyl-3'-{[3-(2-{[2-(2H-1,2,3-triazol-2-yl)benz...

MacromoleculeName: 4'-methoxy-N,N-dimethyl-3'-{[3-(2-{[2-(2H-1,2,3-triazol-2-yl)benzene-1-carbonyl]amino}ethyl)phenyl]sulfamoyl}[1,1'-biphenyl]-3-carboxamide
type: ligand / ID: 7 / Number of copies: 1 / Formula: XGD
Molecular weightTheoretical: 624.709 Da
Chemical component information

ChemComp-XGD:
4'-methoxy-N,N-dimethyl-3'-{[3-(2-{[2-(2H-1,2,3-triazol-2-yl)benzene-1-carbonyl]amino}ethyl)phenyl]sulfamoyl}[1,1'-biphenyl]-3-carboxamide

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration5 mg/mL
BufferpH: 7.6
Component:
ConcentrationFormulaName
25.0 mMTrisTris
50.0 mMNH4OAcammonium acetate
0.02 percentDDMDDM
0.002 percentCHSCHS
0.5 mMEDTAEDTA
GridModel: C-flat-1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Support film - Film thickness: 20.0 nm / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.038 kPa / Details: Carbon side facing up
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV / Details: 3s blot from both sides.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
TemperatureMin: 83.0 K / Max: 93.0 K
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Digitization - Dimensions - Width: 5700 pixel / Digitization - Dimensions - Height: 4100 pixel / Digitization - Sampling interval: 5.0 µm / Number grids imaged: 2 / Number real images: 18000 / Average exposure time: 0.05 sec. / Average electron dose: 1.0625 e/Å2 / Details: 40 frames with total 2s exposure per movie
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Calibrated defocus max: 2.2 µm / Calibrated defocus min: 0.6 µm / Calibrated magnification: 59524 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 105000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 7500000
CTF correctionSoftware - Name: cryoSPARC (ver. 2.15)
Startup modelType of model: OTHER / Details: cryoSPARC ab initio
Final reconstructionNumber classes used: 1 / Applied symmetry - Point group: C1 (asymmetric) / Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 2.15) / Details: Gold standard with masking effect correction / Number images used: 1100000
Initial angle assignmentType: OTHER / Software - Name: cryoSPARC (ver. 2.15) / Details: cryoSPARC
Final angle assignmentType: OTHER / Software - Name: cryoSPARC (ver. 2.15) / Details: cryoSPARC
Final 3D classificationNumber classes: 1 / Avg.num./class: 1100000 / Software - Name: cryoSPARC (ver. 2.15) / Details: One good class

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Atomic model buiding 1

Initial modelPDB ID:

5g53


Chain - Chain ID: C / Details: chain A
RefinementSpace: REAL / Protocol: AB INITIO MODEL / Overall B value: 101 / Target criteria: Correlation
Output model

PDB-7l1v:
Orexin Receptor 2 (OX2R) in Complex with G Protein and Small-Molecule Agonist Compound 1

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Atomic model buiding 2

Initial modelPDB ID:

3sn6


Chain - Chain ID: B / Details: chain B
Output model

PDB-7l1v:
Orexin Receptor 2 (OX2R) in Complex with G Protein and Small-Molecule Agonist Compound 1

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Atomic model buiding 3

Initial modelPDB ID:

3sn6


Chain - Chain ID: G / Details: chain C
Output model

PDB-7l1v:
Orexin Receptor 2 (OX2R) in Complex with G Protein and Small-Molecule Agonist Compound 1

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Atomic model buiding 4

Initial modelPDB ID:

6dde


Chain - Chain ID: E / Details: chain H
Output model

PDB-7l1v:
Orexin Receptor 2 (OX2R) in Complex with G Protein and Small-Molecule Agonist Compound 1

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Atomic model buiding 5

Initial modelPDB ID:

4s0v


Chain - Chain ID: A / Details: chain R
Output model

PDB-7l1v:
Orexin Receptor 2 (OX2R) in Complex with G Protein and Small-Molecule Agonist Compound 1

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