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- EMDB-21685: Structure of human GABA(B) receptor in an inactive state -

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Basic information

Entry
Database: EMDB / ID: EMD-21685
TitleStructure of human GABA(B) receptor in an inactive state
Map dataFinal composite map combining local reconstructions for the extracellular and transmembrane domains. Map was re-sampled in Chimera with pixel spacing 1.1 angstrom.
Sample
  • Complex: Heterodimer human GABA(B) receptor composed of GABA(B1b) and GABA(B2) subunits.
    • Protein or peptide: Gamma-aminobutyric acid type B receptor subunit 1
    • Protein or peptide: Gamma-aminobutyric acid type B receptor subunit 2
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: CALCIUM IONCalcium
  • Ligand: (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-{[(9Z)-octadec-9-enoyl]oxy}propyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
  • Ligand: CHOLESTEROL
  • Ligand: [(2R)-3-[(Z)-icos-11-enoyl]oxy-2-[(Z)-octadec-9-enoyl]oxypropyl] 2-(trimethylazaniumyl)ethyl phosphate
Function / homology
Function and homology information


G protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential / GABA B receptor activation / G protein-coupled neurotransmitter receptor activity involved in regulation of presynaptic membrane potential / G protein-coupled GABA receptor complex / negative regulation of gamma-aminobutyric acid secretion / neuron-glial cell signaling / G protein-coupled GABA receptor activity / G protein-coupled receptor heterodimeric complex / negative regulation of epinephrine secretion / negative regulation of dopamine secretion ...G protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential / GABA B receptor activation / G protein-coupled neurotransmitter receptor activity involved in regulation of presynaptic membrane potential / G protein-coupled GABA receptor complex / negative regulation of gamma-aminobutyric acid secretion / neuron-glial cell signaling / G protein-coupled GABA receptor activity / G protein-coupled receptor heterodimeric complex / negative regulation of epinephrine secretion / negative regulation of dopamine secretion / positive regulation of growth hormone secretion / extracellular matrix protein binding / GABA receptor complex / negative regulation of adenylate cyclase activity / Class C/3 (Metabotropic glutamate/pheromone receptors) / gamma-aminobutyric acid signaling pathway / synaptic transmission, GABAergic / positive regulation of glutamate secretion / negative regulation of synaptic transmission / axolemma / GABA-ergic synapse / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / dendritic shaft / response to nicotine / mitochondrial membrane / Schaffer collateral - CA1 synapse / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / osteoblast differentiation / transmembrane signaling receptor activity / synaptic vesicle / presynaptic membrane / G alpha (i) signalling events / chemical synaptic transmission / postsynaptic membrane / response to ethanol / dendritic spine / neuron projection / G protein-coupled receptor signaling pathway / protein heterodimerization activity / negative regulation of cell population proliferation / neuronal cell body / glutamatergic synapse / endoplasmic reticulum membrane / extracellular space / plasma membrane / cytoplasm
Similarity search - Function
GPCR family 3, gamma-aminobutyric acid receptor, type B2 / Gamma-aminobutyric acid type B receptor subunit 2, coiled-coil domain / Gamma-aminobutyric acid type B receptor subunit 2 coiled-coil domain / GPCR family 3, gamma-aminobutyric acid receptor, type B1 / GPCR family 3, GABA-B receptor / GPCR, family 3, conserved site / G-protein coupled receptors family 3 signature 3. / GPCR, family 3 / GPCR family 3, C-terminal / 7 transmembrane sweet-taste receptor of 3 GCPR ...GPCR family 3, gamma-aminobutyric acid receptor, type B2 / Gamma-aminobutyric acid type B receptor subunit 2, coiled-coil domain / Gamma-aminobutyric acid type B receptor subunit 2 coiled-coil domain / GPCR family 3, gamma-aminobutyric acid receptor, type B1 / GPCR family 3, GABA-B receptor / GPCR, family 3, conserved site / G-protein coupled receptors family 3 signature 3. / GPCR, family 3 / GPCR family 3, C-terminal / 7 transmembrane sweet-taste receptor of 3 GCPR / G-protein coupled receptors family 3 profile. / Sushi repeat (SCR repeat) / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / Sushi/SCR/CCP domain / Sushi/SCR/CCP superfamily / Sushi/CCP/SCR domain profile. / Receptor, ligand binding region / Receptor family ligand binding region / Periplasmic binding protein-like I
Similarity search - Domain/homology
Gamma-aminobutyric acid type B receptor subunit 2 / Gamma-aminobutyric acid type B receptor subunit 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsPark J / Fu Z / Frangaj A / Liu J / Mosyak L / Shen T / Slavkovich VN / Ray KM / Taura J / Cao B ...Park J / Fu Z / Frangaj A / Liu J / Mosyak L / Shen T / Slavkovich VN / Ray KM / Taura J / Cao B / Geng Y / Zuo H / Kou Y / Grassucci R / Chen S / Liu Z / Lin X / Williams JP / Rice WJ / Eng ET / Huang RK / Soni RK / Kloss B / Yu Z / Javitch JA / Hendrickson WA / Slesinger PA / Quick M / Graziano J / Yu H / Fiehn O / Clarke OB / Frank J / Fan QR
Funding support United States, 6 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM088454 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)U2CES030158 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM125801 United States
National Institutes of Health/Office of the DirectorR01GM107462 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)P41GM116799 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)P41GM103310 United States
CitationJournal: Nature / Year: 2020
Title: Structure of human GABA receptor in an inactive state.
Authors: Jinseo Park / Ziao Fu / Aurel Frangaj / Jonathan Liu / Lidia Mosyak / Tong Shen / Vesna N Slavkovich / Kimberly M Ray / Jaume Taura / Baohua Cao / Yong Geng / Hao Zuo / Yongjun Kou / Robert ...Authors: Jinseo Park / Ziao Fu / Aurel Frangaj / Jonathan Liu / Lidia Mosyak / Tong Shen / Vesna N Slavkovich / Kimberly M Ray / Jaume Taura / Baohua Cao / Yong Geng / Hao Zuo / Yongjun Kou / Robert Grassucci / Shaoxia Chen / Zheng Liu / Xin Lin / Justin P Williams / William J Rice / Edward T Eng / Rick K Huang / Rajesh K Soni / Brian Kloss / Zhiheng Yu / Jonathan A Javitch / Wayne A Hendrickson / Paul A Slesinger / Matthias Quick / Joseph Graziano / Hongtao Yu / Oliver Fiehn / Oliver B Clarke / Joachim Frank / Qing R Fan /
Abstract: The human GABA receptor-a member of the class C family of G-protein-coupled receptors (GPCRs)-mediates inhibitory neurotransmission and has been implicated in epilepsy, pain and addiction. A unique ...The human GABA receptor-a member of the class C family of G-protein-coupled receptors (GPCRs)-mediates inhibitory neurotransmission and has been implicated in epilepsy, pain and addiction. A unique GPCR that is known to require heterodimerization for function, the GABA receptor has two subunits, GABA and GABA, that are structurally homologous but perform distinct and complementary functions. GABA recognizes orthosteric ligands, while GABA couples with G proteins. Each subunit is characterized by an extracellular Venus flytrap (VFT) module, a descending peptide linker, a seven-helix transmembrane domain and a cytoplasmic tail. Although the VFT heterodimer structure has been resolved, the structure of the full-length receptor and its transmembrane signalling mechanism remain unknown. Here we present a near full-length structure of the GABA receptor, captured in an inactive state by cryo-electron microscopy. Our structure reveals several ligands that preassociate with the receptor, including two large endogenous phospholipids that are embedded within the transmembrane domains to maintain receptor integrity and modulate receptor function. We also identify a previously unknown heterodimer interface between transmembrane helices 3 and 5 of both subunits, which serves as a signature of the inactive conformation. A unique 'intersubunit latch' within this transmembrane interface maintains the inactive state, and its disruption leads to constitutive receptor activity.
History
DepositionApr 10, 2020-
Header (metadata) releaseJul 1, 2020-
Map releaseJul 1, 2020-
UpdateAug 26, 2020-
Current statusAug 26, 2020Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.6
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.6
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6wiv
  • Surface level: 0.6
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_21685.png

Downloads & links

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Map

FileDownload / File: emd_21685.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationFinal composite map combining local reconstructions for the extracellular and transmembrane domains. Map was re-sampled in Chimera with pixel spacing 1.1 angstrom.
Voxel sizeX=Y=Z: 1.1 Å
Density
Contour LevelBy AUTHOR: 0.5 / Movie #1: 0.6
Minimum - Maximum-0.29351062 - 5.1695056
Average (Standard dev.)0.017307602 (±0.080392115)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 281.6 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.11.11.1
M x/y/z256256256
origin x/y/z0.0000.0000.000
length x/y/z281.600281.600281.600
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ360360360
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS256256256
D min/max/mean-0.2945.1700.017

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Supplemental data

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Additional map: Local reconstruction for the extracellular domain. Map was...

Fileemd_21685_additional_1.map
AnnotationLocal reconstruction for the extracellular domain. Map was re-sampled in Chimera with pixel spacing 1.1 angstrom.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Local reconstruction for the transmembrane domain. Map was...

Fileemd_21685_additional_2.map
AnnotationLocal reconstruction for the transmembrane domain. Map was re-sampled in Chimera with pixel spacing 1.1 angstrom.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Global map without local refinement. Map was re-sampled...

Fileemd_21685_additional_3.map
AnnotationGlobal map without local refinement. Map was re-sampled in Chimera with pixel spacing 1.1 angstrom.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Heterodimer human GABA(B) receptor composed of GABA(B1b) and GABA...

EntireName: Heterodimer human GABA(B) receptor composed of GABA(B1b) and GABA(B2) subunits.
Components
  • Complex: Heterodimer human GABA(B) receptor composed of GABA(B1b) and GABA(B2) subunits.
    • Protein or peptide: Gamma-aminobutyric acid type B receptor subunit 1
    • Protein or peptide: Gamma-aminobutyric acid type B receptor subunit 2
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: CALCIUM IONCalcium
  • Ligand: (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-{[(9Z)-octadec-9-enoyl]oxy}propyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
  • Ligand: CHOLESTEROL
  • Ligand: [(2R)-3-[(Z)-icos-11-enoyl]oxy-2-[(Z)-octadec-9-enoyl]oxypropyl] 2-(trimethylazaniumyl)ethyl phosphate

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Supramolecule #1: Heterodimer human GABA(B) receptor composed of GABA(B1b) and GABA...

SupramoleculeName: Heterodimer human GABA(B) receptor composed of GABA(B1b) and GABA(B2) subunits.
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human) / Recombinant cell: HEK 293 GnTI- / Recombinant plasmid: modified bacMam
Molecular weightExperimental: 193 KDa

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Macromolecule #1: Gamma-aminobutyric acid type B receptor subunit 1

MacromoleculeName: Gamma-aminobutyric acid type B receptor subunit 1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 91.585867 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGPGAPFARV GWPLPLLVVM AAGVAPVWAS HSPHLPRPHS RVPPHPSSER RAVYIGALFP MSGGWPGGQA CQPAVEMALE DVNSRRDIL PDYELKLIHH DSKCDPGQAT KYLYELLYND PIKIILMPGC SSVSTLVAEA ARMWNLIVLS YGSSSPALSN R QRFPTFFR ...String:
MGPGAPFARV GWPLPLLVVM AAGVAPVWAS HSPHLPRPHS RVPPHPSSER RAVYIGALFP MSGGWPGGQA CQPAVEMALE DVNSRRDIL PDYELKLIHH DSKCDPGQAT KYLYELLYND PIKIILMPGC SSVSTLVAEA ARMWNLIVLS YGSSSPALSN R QRFPTFFR THPSATLHNP TRVKLFEKWG WKKIATIQQT TEVFTSTLDD LEERVKEAGI EITFRQSFFS DPAVPVKNLK RQ DARIIVG LFYETEARKV FCEVYKERLF GKKYVWFLIG WYADNWFKIY DPSINCTVDE MTEAVEGHIT TEIVMLNPAN TRS ISNMTS QEFVEKLTKR LKRHPEETGG FQEAPLAYDA IWALALALNK TSGGGGRSGV RLEDFNYNNQ TITDQIYRAM NSSS FEGVS GHVVFDASGS RMAWTLIEQL QGGSYKKIGY YDSTKDDLSW SKTDKWIGGS PPADQTLVIK TFRFLSQKLF ISVSV LSSL GIVLAVVCLS FNIYNSHVRY IQNSQPNLNN LTAVGCSLAL AAVFPLGLDG YHIGRNQFPF VCQARLWLLG LGFSLG YGS MFTKIWWVHT VFTKKEEKKE WRKTLEPWKL YATVGLLVGM DVLTLAIWQI VDPLHRTIET FAKEEPKEDI DVSILPQ LE HCSSRKMNTW LGIFYGYKGL LLLLGIFLAY ETKSVSTEKI NDHRAVGMAI YNVAVLCLIT APVTMILSSQ QDAAFAFA S LAIVFSSYIT LVVLFVPKMR RLITRGEWQS EAQDTMKTGS STNNNEEEKS RLLEKENREL EKIIAEKEER VSELRHQLQ SRDYKDDDDK

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Macromolecule #2: Gamma-aminobutyric acid type B receptor subunit 2

MacromoleculeName: Gamma-aminobutyric acid type B receptor subunit 2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 93.278781 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MASPRSSGQP GPPPPPPPPP ARLLLLLLLP LLLPLAPGAW GWARGAPRPP PSSPPLSIMG LMPLTKEVAK GSIGRGVLPA VELAIEQIR NESLLRPYFL DLRLYDTECD NAKGLKAFYD AIKYGPNHLM VFGGVCPSVT SIIAESLQGW NLVQLSFAAT T PVLADKKK ...String:
MASPRSSGQP GPPPPPPPPP ARLLLLLLLP LLLPLAPGAW GWARGAPRPP PSSPPLSIMG LMPLTKEVAK GSIGRGVLPA VELAIEQIR NESLLRPYFL DLRLYDTECD NAKGLKAFYD AIKYGPNHLM VFGGVCPSVT SIIAESLQGW NLVQLSFAAT T PVLADKKK YPYFFRTVPS DNAVNPAILK LLKHYQWKRV GTLTQDVQRF SEVRNDLTGV LYGEDIEISD TESFSNDPCT SV KKLKGND VRIILGQFDQ NMAAKVFCCA YEENMYGSKY QWIIPGWYEP SWWEQVHTEA NSSRCLRKNL LAAMEGYIGV DFE PLSSKQ IKTISGKTPQ QYEREYNNKR SGVGPSKFHG YAYDGIWVIA KTLQRAMETL HASSRHQRIQ DFNYTDHTLG RIIL NAMNE TNFFGVTGQV VFRNGERMGT IKFTQFQDSR EVKVGEYNAV ADTLEIINDT IRFQGSEPPK DKTIILEQLR KISLP LYSI LSALTILGMI MASAFLFFNI KNRNQKLIKM SSPYMNNLII LGGMLSYASI FLFGLDGSFV SEKTFETLCT VRTWIL TVG YTTAFGAMFA KTWRVHAIFK NVKMKKKIIK DQKLLVIVGG MLLIDLCILI CWQAVDPLRR TVEKYSMEPD PAGRDIS IR PLLEHCENTH MTIWLGIVYA YKGLLMLFGC FLAWETRNVS IPALNDSKYI GMSVYNVGIM CIIGAAVSFL TRDQPNVQ F CIVALVIIFC STITLCLVFV PKLITLRTNP DAATQNRRFQ FTQNQKKEDS KTSTSVTSVN QASTSRLEGL QSENHRLRM KITELDKDLE EVTMQLQDTD YKDDDDK

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Macromolecule #3: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 3 / Number of copies: 4 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

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Macromolecule #4: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 4 / Number of copies: 1 / Formula: CA
Molecular weightTheoretical: 40.078 Da

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Macromolecule #5: (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-{[(9Z)-oct...

MacromoleculeName: (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-{[(9Z)-octadec-9-enoyl]oxy}propyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
type: ligand / ID: 5 / Number of copies: 1 / Formula: U3G
Molecular weightTheoretical: 766.039 Da
Chemical component information

ChemComp-U3G:
(2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-{[(9Z)-octadec-9-enoyl]oxy}propyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate

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Macromolecule #6: CHOLESTEROL

MacromoleculeName: CHOLESTEROL / type: ligand / ID: 6 / Number of copies: 10 / Formula: CLR
Molecular weightTheoretical: 386.654 Da
Chemical component information

ChemComp-CLR:
CHOLESTEROL / Cholesterol

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Macromolecule #7: [(2R)-3-[(Z)-icos-11-enoyl]oxy-2-[(Z)-octadec-9-enoyl]oxypropyl] ...

MacromoleculeName: [(2R)-3-[(Z)-icos-11-enoyl]oxy-2-[(Z)-octadec-9-enoyl]oxypropyl] 2-(trimethylazaniumyl)ethyl phosphate
type: ligand / ID: 7 / Number of copies: 1 / Formula: U3D
Molecular weightTheoretical: 814.167 Da
Chemical component information

ChemComp-U3D:
[(2R)-3-[(Z)-icos-11-enoyl]oxy-2-[(Z)-octadec-9-enoyl]oxypropyl] 2-(trimethylazaniumyl)ethyl phosphate

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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

Concentration0.3 mg/mL
BufferpH: 7.5
Component:
ConcentrationFormulaName
50.0 mMC8H18N2O4SHEPES
50.0 mMNaClSodium chloridesodium chloride
0.002 %C47H88O22Lauryl Maltose Neopentyl Glycol
0.0004 %C31H50O4Cholesteryl Hemisuccinate

Details: Solutions were made fresh from concentrated and filtered to avoid microbial contamination.
GridModel: Quantifoil R0.6/1 / Material: GOLD / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Support film - Film thickness: 50.0 nm / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Atmosphere: OTHER
VitrificationCryogen name: ETHANE-PROPANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV / Details: blot for 4 seconds before plunging.
DetailsThis sample was monodisperse

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: -2.0 µm / Nominal defocus min: -0.5 µm / Nominal magnification: 130000
Specialist opticsEnergy filter - Slit width: 20 eV
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
TemperatureMax: 100.0 K
DetailsPreliminary grid screening was performed manually.
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Digitization - Frames/image: 1-60 / Number grids imaged: 1 / Number real images: 3435 / Average exposure time: 12.0 sec. / Average electron dose: 85.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 1048241
CTF correctionSoftware - Name: Gctf (ver. 1.06)
Startup modelType of model: OTHER / Details: Ab initio (cryoSPARC 2)
Initial angle assignmentType: OTHER / Software - Name: cryoSPARC (ver. 2) / Software - details: Non-uniform refinement
Final angle assignmentType: OTHER / Software - Name: cryoSPARC (ver. 2)
Details: Non-uniform refinement and local refinement in cryoSPARC 2
Final reconstructionNumber classes used: 1 / Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 2) / Number images used: 233737

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Atomic model buiding 1

Initial model
PDB IDChain

4mqe

chain_id: A, residue_range: 48-459

4mqe

chain_id: B, residue_range: 53-466
RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-6wiv:
Structure of human GABA(B) receptor in an inactive state

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