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- EMDB-51284: Structure of GPR55 in complex with G13 and synthetic agonist ML184 -

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Entry
Database: EMDB / ID: EMD-51284
TitleStructure of GPR55 in complex with G13 and synthetic agonist ML184
Map data
Sample
  • Complex: Structure of GPR55 in complex with G13 and synthetic agonist ML184
    • Complex: Guanine nucleotide-binding proteins
      • Protein or peptide: Guanine nucleotide-binding protein subunit alpha-13
      • 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
    • Complex: Single-chain variable fragment ScFv16
      • Protein or peptide: Single-chain variable fragment ScFv16
    • Complex: G-protein coupled receptor 55 with a GFP tag
      • Protein or peptide: Green fluorescent protein,G-protein coupled receptor 55
  • Ligand: 3-[4-(2,3-dimethylphenyl)piperazin-1-yl]carbonyl-N,N-dimethyl-4-pyrrolidin-1-yl-benzenesulfonamide
  • Ligand: CHOLESTEROL
  • Ligand: water
KeywordsG protein-coupled receptor / GPCR / lipid agonist / cholesterol / MEMBRANE PROTEIN
Function / homology
Function and homology information


D5 dopamine receptor binding / Rho-activating G protein-coupled receptor signaling pathway / regulation of fibroblast migration / cannabinoid receptor activity / Class A/1 (Rhodopsin-like receptors) / regulation of small GTPase mediated signal transduction / NRAGE signals death through JNK / branching involved in blood vessel morphogenesis / positive regulation of Rho protein signal transduction / negative regulation of vascular associated smooth muscle cell migration ...D5 dopamine receptor binding / Rho-activating G protein-coupled receptor signaling pathway / regulation of fibroblast migration / cannabinoid receptor activity / Class A/1 (Rhodopsin-like receptors) / regulation of small GTPase mediated signal transduction / NRAGE signals death through JNK / branching involved in blood vessel morphogenesis / positive regulation of Rho protein signal transduction / negative regulation of vascular associated smooth muscle cell migration / negative regulation of osteoclast differentiation / negative regulation of vascular associated smooth muscle cell proliferation / CDC42 GTPase cycle / regulation of postsynapse assembly / Rho protein signal transduction / bone resorption / RAC1 GTPase cycle / bioluminescence / guanyl-nucleotide exchange factor activity / generation of precursor metabolites and energy / brush border membrane / G protein-coupled receptor activity / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / regulation of blood pressure / platelet activation / G-protein beta/gamma-subunit complex 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-coupled acetylcholine receptor signaling pathway / adenylate cyclase-activating G protein-coupled receptor signaling pathway / G-protein activation / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / Prostacyclin signalling through prostacyclin receptor / G beta:gamma signalling through CDC42 / Glucagon signaling in metabolic regulation / G beta:gamma signalling through BTK / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / ADP signalling through P2Y purinoceptor 12 / Sensory perception of sweet, bitter, and umami (glutamate) taste / photoreceptor disc membrane / Glucagon-type ligand receptors / Adrenaline,noradrenaline inhibits insulin secretion / Vasopressin regulates renal water homeostasis via Aquaporins / G alpha (z) signalling events / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / ADORA2B mediated anti-inflammatory cytokines production / cellular response to catecholamine stimulus / ADP signalling through P2Y purinoceptor 1 / G beta:gamma signalling through PI3Kgamma / adenylate cyclase-activating dopamine receptor signaling pathway / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / GPER1 signaling / Inactivation, recovery and regulation of the phototransduction cascade / cellular response to prostaglandin E stimulus / G-protein beta-subunit binding / heterotrimeric G-protein complex / melanosome / G alpha (12/13) signalling events / sensory perception of taste / extracellular vesicle / signaling receptor complex adaptor activity / regulation of cell shape / Thrombin signalling through proteinase activated receptors (PARs) / G protein activity / GTPase binding / Ca2+ pathway / positive regulation of cytosolic calcium ion concentration / retina development in camera-type eye / High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells / fibroblast proliferation / G alpha (i) signalling events / G alpha (s) signalling events / phospholipase C-activating G protein-coupled receptor signaling pathway / G alpha (q) signalling events / in utero embryonic development / Ras protein signal transduction / cell differentiation / Extra-nuclear estrogen signaling / cell population proliferation / postsynapse / positive regulation of ERK1 and ERK2 cascade / G protein-coupled receptor signaling pathway / lysosomal membrane / focal adhesion / GTPase activity / synapse / protein-containing complex binding / GTP binding / signal transduction / extracellular exosome / metal ion binding / nucleus / membrane / plasma membrane / cytosol / cytoplasm
Similarity search - Function
G-protein alpha subunit, group 12/13 / Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / Guanine nucleotide binding protein (G-protein), alpha subunit / G protein alpha subunit, helical insertion / G-protein alpha subunit / G-alpha domain profile. / G protein alpha subunit ...G-protein alpha subunit, group 12/13 / Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / Guanine nucleotide binding protein (G-protein), alpha subunit / G protein alpha subunit, helical insertion / G-protein alpha subunit / G-alpha domain profile. / G protein alpha subunit / G-protein, gamma subunit / G-protein gamma subunit domain profile. / G-protein gamma-like domain / G-protein gamma-like domain superfamily / GGL domain / G protein gamma subunit-like motifs / GGL domain / 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. / WD domain, G-beta repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Green fluorescent protein / 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 / Guanine nucleotide-binding protein subunit alpha-13 / G-protein coupled receptor 55
Similarity search - Component
Biological speciesHomo sapiens (human) / Mus musculus (house mouse) / Aequorea victoria (jellyfish)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.51 Å
AuthorsClaff T / Ebenhoch R / Weichert D
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: Nat Commun / Year: 2025
Title: Structural basis for lipid-mediated activation of G protein-coupled receptor GPR55.
Authors: Tobias Claff / Rebecca Ebenhoch / Jörg T Kley / Aniket Magarkar / Herbert Nar / Dietmar Weichert /
Abstract: GPR55 is an orphan G protein-coupled receptor (GPCR) and represents a promising drug target for cancer, inflammation, and metabolic diseases. The endogenous activation of lipid GPCRs can be solely ...GPR55 is an orphan G protein-coupled receptor (GPCR) and represents a promising drug target for cancer, inflammation, and metabolic diseases. The endogenous activation of lipid GPCRs can be solely mediated by membrane components and different lipids have been proposed as endogenous activators of GPR55, such as cannabinoids and lysophosphatidylinositols. Here, we determine high-resolution cryo-electron microscopy structures of the activated GPR55 in complex with heterotrimeric G and two structurally diverse ligands: the putative endogenous agonist 1-palmitoyl-2-lysophosphatidylinositol (LPI) and the synthetic agonist ML184. These results reveal insights into ligand recognition at GPR55, G protein coupling and receptor activation. Notably, an orthosteric binding site opening towards the membrane is observed in both structures, enabling direct interaction of the agonists with membrane lipids. The structural observations are supported by mutagenesis and functional experiments employing G protein dissociation assays. These findings will be of importance for the structure-based development of drugs targeting GPR55.
History
DepositionAug 6, 2024-
Header (metadata) releaseMar 5, 2025-
Map releaseMar 5, 2025-
UpdateMar 5, 2025-
Current statusMar 5, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_51284.png

Downloads & links

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Map

FileDownload / File: emd_51284.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesX (Sec.)Y (Row.)Z (Col.)
0.83 Å/pix.
x 320 pix.
= 265.28 Å		0.83 Å/pix.
x 320 pix.
= 265.28 Å		0.83 Å/pix.
x 320 pix.
= 265.28 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.829 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 8.0
Minimum - Maximum-56.282089999999997 - 77.674469999999999
Average (Standard dev.)-0.0074139005 (±1.1039947)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 265.28 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Structure of GPR55 in complex with G13 and synthetic agonist ML184

EntireName: Structure of GPR55 in complex with G13 and synthetic agonist ML184
Components
  • Complex: Structure of GPR55 in complex with G13 and synthetic agonist ML184
    • Complex: Guanine nucleotide-binding proteins
      • Protein or peptide: Guanine nucleotide-binding protein subunit alpha-13
      • 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
    • Complex: Single-chain variable fragment ScFv16
      • Protein or peptide: Single-chain variable fragment ScFv16
    • Complex: G-protein coupled receptor 55 with a GFP tag
      • Protein or peptide: Green fluorescent protein,G-protein coupled receptor 55
  • Ligand: 3-[4-(2,3-dimethylphenyl)piperazin-1-yl]carbonyl-N,N-dimethyl-4-pyrrolidin-1-yl-benzenesulfonamide
  • Ligand: CHOLESTEROL
  • Ligand: water

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Supramolecule #1: Structure of GPR55 in complex with G13 and synthetic agonist ML184

SupramoleculeName: Structure of GPR55 in complex with G13 and synthetic agonist ML184
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5
Molecular weightTheoretical: 180 KDa

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Supramolecule #2: Guanine nucleotide-binding proteins

SupramoleculeName: Guanine nucleotide-binding proteins / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#2, #4
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #3: Single-chain variable fragment ScFv16

SupramoleculeName: Single-chain variable fragment ScFv16 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #3
Source (natural)Organism: Mus musculus (house mouse)

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Supramolecule #4: G-protein coupled receptor 55 with a GFP tag

SupramoleculeName: G-protein coupled receptor 55 with a GFP tag / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #5
Source (natural)Organism: Aequorea victoria (jellyfish)

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Macromolecule #1: Guanine nucleotide-binding protein subunit alpha-13

MacromoleculeName: Guanine nucleotide-binding protein subunit alpha-13 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 26.5744 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MGSTVSAEDK AAAERSKEID KCLSREKTYV KRLVKILLLG ADNSGKSTFL KQMRIIHGGS GGSGGTKGIH EYDFEIKNVP FKMVDVGGQ RSERKRWFEC FDSVTSILFL VDSSDFNRLT ESLNDFETIV NNRVFSNVSI ILFLNKTDLL EEKVQIVSIK D YFLEFEGD ...String:
MGSTVSAEDK AAAERSKEID KCLSREKTYV KRLVKILLLG ADNSGKSTFL KQMRIIHGGS GGSGGTKGIH EYDFEIKNVP FKMVDVGGQ RSERKRWFEC FDSVTSILFL VDSSDFNRLT ESLNDFETIV NNRVFSNVSI ILFLNKTDLL EEKVQIVSIK D YFLEFEGD PHCLRDVQKF LVECFRNKRR DQQQKPLYHH FTTAINTENA RLIFRDVKDT ILHDNLKQLM LQ

UniProtKB: Guanine nucleotide-binding protein subunit alpha-13, Guanine nucleotide-binding protein subunit alpha-13

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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: 39.418086 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MHHHHHHLEV LFQGPGSSGS ELDQLRQEAE QLKNQIRDAR KACADATLSQ ITNNIDPVGR IQMRTRRTLR GHLAKIYAMH WGTDSRLLV SASQDGKLII WDSYTTNKVH AIPLRSSWVM TCAYAPSGNY VACGGLDNIC SIYNLKTREG NVRVSRELAG H TGYLSCCR ...String:
MHHHHHHLEV LFQGPGSSGS ELDQLRQEAE QLKNQIRDAR KACADATLSQ ITNNIDPVGR IQMRTRRTLR GHLAKIYAMH WGTDSRLLV SASQDGKLII WDSYTTNKVH AIPLRSSWVM TCAYAPSGNY VACGGLDNIC SIYNLKTREG NVRVSRELAG H TGYLSCCR FLDDNQIVTS SGDTTCALWD IETGQQTTTF TGHTGDVMSL SLAPDTRLFV SGACDASAKL WDVREGMCRQ TF TGHESDI NAICFFPNGN AFATGSDDAT CRLFDLRADQ ELMTYSHDNI ICGITSVSFS KSGRLLLAGY DDFNCNVWDA LKA DRAGVL AGHDNRVSCL GVTDDGMAVA TGSWDSFLKI WN

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

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Macromolecule #3: Single-chain variable fragment ScFv16

MacromoleculeName: Single-chain variable fragment ScFv16 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 27.068225 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: DVQLVESGGG LVQPGGSRKL SCSASGFAFS SFGMHWVRQA PEKGLEWVAY ISSGSGTIYY ADTVKGRFTI SRDDPKNTLF LQMTSLRSE DTAMYYCVRS IYYYGSSPFD FWGGTTLTVS SGGGGSGGGG SGGGGSDIVM TQATSSVPVT PGESVSISCR S SKSLLHSN ...String:
DVQLVESGGG LVQPGGSRKL SCSASGFAFS SFGMHWVRQA PEKGLEWVAY ISSGSGTIYY ADTVKGRFTI SRDDPKNTLF LQMTSLRSE DTAMYYCVRS IYYYGSSPFD FWGGTTLTVS SGGGGSGGGG SGGGGSDIVM TQATSSVPVT PGESVSISCR S SKSLLHSN GNTYLYWFLQ RPGQSPQLLI YRMSNLASGV PDRFSGSGSG TAFTLTISRL EAEDVGVYYC MQHLEYPLTF GA GTKLELK LEVLFQ

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Macromolecule #4: 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: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.506765 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
MASNNTASIA QARKLVEQLK MEANIDRIKV SKAAADLMAY CEAHAKEDPL LTPVPASENP FREKKFFCAI LGSAGSAGSA

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

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Macromolecule #5: Green fluorescent protein,G-protein coupled receptor 55

MacromoleculeName: Green fluorescent protein,G-protein coupled receptor 55
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 73.124812 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MKTIIALSYI FCLVFADYKD DDDKKGEELF TGVVPILVEL DGDVNGHKFS VSGEGEGDAT YGKLTLKFIC TTGKLPVPWP TLVTTLTYG VQCFSRYPDH MKRHDFFKSA MPEGYVQERT ISFKDDGNYK TRAEVKFEGD TLVNRIELKG IDFKEDGNIL G HKLEYNYN ...String:
MKTIIALSYI FCLVFADYKD DDDKKGEELF TGVVPILVEL DGDVNGHKFS VSGEGEGDAT YGKLTLKFIC TTGKLPVPWP TLVTTLTYG VQCFSRYPDH MKRHDFFKSA MPEGYVQERT ISFKDDGNYK TRAEVKFEGD TLVNRIELKG IDFKEDGNIL G HKLEYNYN SHNVYITADK QKNGIKANFK IRHNIEDGSV QLADHYQQNT PIGDGPVLLP DNHYLSTQSA LSKDPNEKRD HM VLLEFVT AAGITHGMDE LYKAAGSGEF LEVLFQGPGA GSDSMSQQNT SGDCLFDGVN ELMKTLQFAV HIPTFVLGLL LNL LAIHGF STFLKNRWPD YAATSIYMIN LAVFDLLLVL SLPFKMVLSQ VQSPFPSLCT LVECLYFVSM YGSVFTICFI SMDR FLAIR YPLLVSHLRS PRKIFGICCT IWVLVWTGSI PIYSFHGKVE KYMCFHNMSD DTWSAKVFFP LEVFGFLLPM GIMGF CCSR SIHILLGRRD HTQDWVQQKA CIYSIAASLA VFVVSFLPVH LGFFLQFLVR NSFIVECRAK QSISFFLQLS MCFSNV NCC LDVFCYYFVI KEFRMNIRAH RPSRVQLVLQ DTTISRGAGS GAGSAWSHPQ FEKGGGSGGG SGGSAWSHPQ FEKGAGS HH HHHHHHHH

UniProtKB: Green fluorescent protein, G-protein coupled receptor 55

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Macromolecule #7: 3-[4-(2,3-dimethylphenyl)piperazin-1-yl]carbonyl-N,N-dimethyl-4-p...

MacromoleculeName: 3-[4-(2,3-dimethylphenyl)piperazin-1-yl]carbonyl-N,N-dimethyl-4-pyrrolidin-1-yl-benzenesulfonamide
type: ligand / ID: 7 / Number of copies: 1 / Formula: A1IKH
Molecular weightTheoretical: 470.627 Da

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Macromolecule #8: CHOLESTEROL

MacromoleculeName: CHOLESTEROL / type: ligand / ID: 8 / Number of copies: 1 / Formula: CLR
Molecular weightTheoretical: 386.654 Da
Chemical component information

ChemComp-CLR:
CHOLESTEROL

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Macromolecule #9: water

MacromoleculeName: water / type: ligand / ID: 9 / Number of copies: 14 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER

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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

BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 45.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 105000
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 15173387
Startup modelType of model: NONE
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 2.51 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 829193
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC

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