[English] 日本語
Yorodumi
- PDB-9tpq: GABA-A receptor a3b3g2 + a3NB77 + GABA -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 9tpq
TitleGABA-A receptor a3b3g2 + a3NB77 + GABA
Components
  • (Gamma-aminobutyric acid receptor subunit ...) x 3
  • a3NB77
KeywordsMEMBRANE PROTEIN / pLGIC / GABA / Neurotransmission
Function / homology
Function and homology information


benzodiazepine receptor activity / extrasynaptic signaling via GABA / cellular response to histamine / inner ear receptor cell development / GABA receptor activation / negative regulation of synaptic transmission, GABAergic / innervation / GABA-gated chloride ion channel activity / GABA-A receptor complex / inhibitory synapse assembly ...benzodiazepine receptor activity / extrasynaptic signaling via GABA / cellular response to histamine / inner ear receptor cell development / GABA receptor activation / negative regulation of synaptic transmission, GABAergic / innervation / GABA-gated chloride ion channel activity / GABA-A receptor complex / inhibitory synapse assembly / GABA-A receptor activity / roof of mouth development / inhibitory postsynaptic potential / synaptic transmission, GABAergic / gamma-aminobutyric acid signaling pathway / postsynaptic specialization membrane / chloride channel activity / Signaling by ERBB4 / cochlea development / chloride channel complex / cytoplasmic vesicle membrane / dendrite membrane / chloride transmembrane transport / electron transport chain / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / GABA-ergic synapse / dendritic spine / electron transfer activity / periplasmic space / postsynaptic membrane / postsynapse / iron ion binding / axon / heme binding / cell surface / signal transduction / identical protein binding / plasma membrane
Similarity search - Function
Gamma-aminobutyric-acid A receptor, alpha 3 subunit / Gamma-aminobutyric-acid A receptor, gamma 2 subunit / Gamma-aminobutyric acid receptor subunit gamma-1/4 / Gamma-aminobutyric-acid A receptor, alpha subunit / : / Gamma-aminobutyric-acid A receptor, beta subunit / Gamma-aminobutyric acid A receptor/Glycine receptor alpha / Neurotransmitter-gated ion-channel, conserved site / Neurotransmitter-gated ion-channels signature. / Neurotransmitter-gated ion-channel transmembrane domain ...Gamma-aminobutyric-acid A receptor, alpha 3 subunit / Gamma-aminobutyric-acid A receptor, gamma 2 subunit / Gamma-aminobutyric acid receptor subunit gamma-1/4 / Gamma-aminobutyric-acid A receptor, alpha subunit / : / Gamma-aminobutyric-acid A receptor, beta subunit / Gamma-aminobutyric acid A receptor/Glycine receptor alpha / Neurotransmitter-gated ion-channel, conserved site / Neurotransmitter-gated ion-channels signature. / Neurotransmitter-gated ion-channel transmembrane domain / Neurotransmitter-gated ion-channel transmembrane region / Cytochrome b562 / Cytochrome b562 / Cytochrome c/b562 / Neurotransmitter-gated ion-channel transmembrane domain superfamily / Neuronal acetylcholine receptor / Neurotransmitter-gated ion-channel / Neurotransmitter-gated ion-channel ligand-binding domain / Neurotransmitter-gated ion-channel ligand-binding domain superfamily / Neurotransmitter-gated ion-channel ligand binding domain
Similarity search - Domain/homology
GAMMA-AMINO-BUTANOIC ACID / Soluble cytochrome b562 / Gamma-aminobutyric acid receptor subunit gamma-2 / Gamma-aminobutyric acid receptor subunit beta-3 / Gamma-aminobutyric acid receptor subunit alpha-3
Similarity search - Component
Biological speciesHomo sapiens (human)
Escherichia coli (E. coli)
Lama glama (llama)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsShang, C. / Nestorow, S.A. / Miller, P.S.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Biotechnology and Biological Sciences Research Council (BBSRC)BB/M024709/1 United Kingdom
CitationJournal: Sci Adv / Year: 2026
Title: Determining the molecular and physiological actions of subtype-selective nanobodies of GABA receptors.
Authors: Jose Enrique Gonzalez-Prada / Sulin Liu / Chuhan Shang / Chloe S Chernoff / Damian P Bright / Martin Mortensen / Charlotte F Jones / Stephanie Nestorow / Vikram Babu Kasaragod / Wan-Na Chen ...Authors: Jose Enrique Gonzalez-Prada / Sulin Liu / Chuhan Shang / Chloe S Chernoff / Damian P Bright / Martin Mortensen / Charlotte F Jones / Stephanie Nestorow / Vikram Babu Kasaragod / Wan-Na Chen / Saad Hannan / Jianchong Zhou / Alexander W E Dunn / Asma Soltani / Richard J Turner / Natasha M Duggan / Yin Yuan / Ayla A Wahid / Steven W Hardwick / Suzanne Scott / Dimitri Y Chirgadze / Els Pardon / Jan Steyaert / A Radu Aricescu / Ole Paulsen / David Belin / Trevor G Smart / Paul S Miller /
Abstract: γ-Aminobutyric acid type-A (GABA) receptors are the principal mediators of inhibitory neurotransmission in the human central nervous system. The α- and α-containing subtypes have tightly ...γ-Aminobutyric acid type-A (GABA) receptors are the principal mediators of inhibitory neurotransmission in the human central nervous system. The α- and α-containing subtypes have tightly controlled spatial expression profiles, which influence anxiety, nociception, epilepsy, and autism. α/α-Selective small molecules compromise on strength of effect (efficacy) to avoid off-subtype modulation. To break this pharmacological deadlock, we study here a panel of nanobodies (NBs) raised against α- and α-containing GABA receptors. We identify subtype selective silent binders, positive allosteric modulators (PAMs), and inhibitors. Cryo-electron microscopy structures explain the binding modes and molecular mechanisms of action of representative NBs. Modulators exhibit distinct synaptic and extrasynaptic functional profiles in brain slices and neuronal networks and can reduce anxiety in vivo. These selective and efficacious NBs (whether inhibitors or positive modulators) enable strong yet precise pharmacological control of α/α-containing subtypes to advance basic research and as potential therapeutic leads to treat neuropsychiatric disorders.
History
DepositionDec 18, 2025Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 26, 2026Provider: repository / Type: Initial release
Revision 1.0Aug 26, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Gamma-aminobutyric acid receptor subunit alpha-3
B: Gamma-aminobutyric acid receptor subunit beta-3,Soluble cytochrome b562
C: Gamma-aminobutyric acid receptor subunit gamma-2
D: Gamma-aminobutyric acid receptor subunit alpha-3
E: Gamma-aminobutyric acid receptor subunit beta-3,Soluble cytochrome b562
F: a3NB77
G: a3NB77
hetero molecules


Theoretical massNumber of molelcules
Total (without water)266,43620
Polymers259,9837
Non-polymers6,45313
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

-
Components

-
Gamma-aminobutyric acid receptor subunit ... , 3 types, 5 molecules ADBEC

#1: Protein Gamma-aminobutyric acid receptor subunit alpha-3 / GABA(A) receptor subunit alpha-3 / GABAAR subunit alpha-3


Mass: 43382.766 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: Glvi linker sequence (SQPARAA). Region substituted: Arg337-Ser425,Glvi linker sequence (SQPARAA). Region substituted: Arg337-Ser425,Glvi linker sequence (SQPARAA). Region substituted: Arg337- ...Details: Glvi linker sequence (SQPARAA). Region substituted: Arg337-Ser425,Glvi linker sequence (SQPARAA). Region substituted: Arg337-Ser425,Glvi linker sequence (SQPARAA). Region substituted: Arg337-Ser425,Glvi linker sequence (SQPARAA). Region substituted: Arg337-Ser425,Glvi linker sequence (SQPARAA). Region substituted: Arg337-Ser425,Glvi linker sequence (SQPARAA). Region substituted: Arg337-Ser425,Glvi linker sequence (SQPARAA). Region substituted: Arg337-Ser425,Glvi linker sequence (SQPARAA). Region substituted: Arg337-Ser425
Source: (gene. exp.) Homo sapiens (human) / Gene: GABRA3 / Production host: Homo sapiens (human) / References: UniProt: P34903
#2: Protein Gamma-aminobutyric acid receptor subunit beta-3,Soluble cytochrome b562 / GABA(A) receptor subunit beta-3 / GABAAR subunit beta-3 / Cytochrome b-562


Mass: 51615.117 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: Modified glvi sequence containing the Escherichia coli soluble cytochrome B562RIL41 (BRIL, amino acids 23-130, ADLE...QKYL, Uniprot P0ABE7) to give the sequence SQPAGT-BRIL-TGRAA. Linker ...Details: Modified glvi sequence containing the Escherichia coli soluble cytochrome B562RIL41 (BRIL, amino acids 23-130, ADLE...QKYL, Uniprot P0ABE7) to give the sequence SQPAGT-BRIL-TGRAA. Linker regions substituted Gly308-Asn421. This BRIL domain was present in the protein but not resolved in the cryo-EM density and is therefore not included in the atomic model.,Modified glvi sequence containing the Escherichia coli soluble cytochrome B562RIL41 (BRIL, amino acids 23-130, ADLE...QKYL, Uniprot P0ABE7) to give the sequence SQPAGT-BRIL-TGRAA. Linker regions substituted Gly308-Asn421. This BRIL domain was present in the protein but not resolved in the cryo-EM density and is therefore not included in the atomic model.,Modified glvi sequence containing the Escherichia coli soluble cytochrome B562RIL41 (BRIL, amino acids 23-130, ADLE...QKYL, Uniprot P0ABE7) to give the sequence SQPAGT-BRIL-TGRAA. Linker regions substituted Gly308-Asn421. This BRIL domain was present in the protein but not resolved in the cryo-EM density and is therefore not included in the atomic model.
Source: (gene. exp.) Homo sapiens (human), (gene. exp.) Escherichia coli (E. coli)
Gene: GABRB3, cybC / Production host: Homo sapiens (human) / References: UniProt: P28472, UniProt: P0ABE7
#3: Protein Gamma-aminobutyric acid receptor subunit gamma-2 / GABA(A) receptor subunit gamma-2 / GABAAR subunit gamma-2


Mass: 42798.875 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: Includes an 1D4 tag at C-terminus of the sequence (TETSQVAPA), this is not resolved in density and not modelled. Glvi linker sequence (SQPARAA), region substituted Ser322-Ala408,Includes an ...Details: Includes an 1D4 tag at C-terminus of the sequence (TETSQVAPA), this is not resolved in density and not modelled. Glvi linker sequence (SQPARAA), region substituted Ser322-Ala408,Includes an 1D4 tag at C-terminus of the sequence (TETSQVAPA), this is not resolved in density and not modelled. Glvi linker sequence (SQPARAA), region substituted Ser322-Ala408,Includes an 1D4 tag at C-terminus of the sequence (TETSQVAPA), this is not resolved in density and not modelled. Glvi linker sequence (SQPARAA), region substituted Ser322-Ala408,Includes an 1D4 tag at C-terminus of the sequence (TETSQVAPA), this is not resolved in density and not modelled. Glvi linker sequence (SQPARAA), region substituted Ser322-Ala408,Includes an 1D4 tag at C-terminus of the sequence (TETSQVAPA), this is not resolved in density and not modelled. Glvi linker sequence (SQPARAA), region substituted Ser322-Ala408,Includes an 1D4 tag at C-terminus of the sequence (TETSQVAPA), this is not resolved in density and not modelled. Glvi linker sequence (SQPARAA), region substituted Ser322-Ala408,Includes an 1D4 tag at C-terminus of the sequence (TETSQVAPA), this is not resolved in density and not modelled. Glvi linker sequence (SQPARAA), region substituted Ser322-Ala408,Includes an 1D4 tag at C-terminus of the sequence (TETSQVAPA), this is not resolved in density and not modelled. Glvi linker sequence (SQPARAA), region substituted Ser322-Ala408
Source: (gene. exp.) Homo sapiens (human) / Gene: GABRG2 / Production host: Homo sapiens (human) / References: UniProt: P18507

-
Antibody / Non-polymers , 2 types, 4 molecules FG

#10: Chemical ChemComp-ABU / GAMMA-AMINO-BUTANOIC ACID / GAMMA(AMINO)-BUTYRIC ACID


Mass: 103.120 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H9NO2 / Feature type: SUBJECT OF INVESTIGATION / Comment: neurotransmitter, inhibitor*YM
#4: Antibody a3NB77


Mass: 13594.054 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lama glama (llama) / Production host: Homo sapiens (human)

-
Sugars , 5 types, 11 molecules

#5: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1235.105 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,7,6/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1_e6-g1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#6: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}LINUCSPDB-CARE
#7: Polysaccharide alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D- ...alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1072.964 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#8: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}LINUCSPDB-CARE
#9: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

-
Details

Has ligand of interestY
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

Component
IDNameTypeDetails (eV)Entity IDParent-IDSource
1alpha3-beta3-gamma2 GABA-A receptor in complex with GABA and nanobody a3NB77COMPLEXThe heteropentameric alpha3beta3gamma2 GABA(A) receptor was recombinantly expressed in HEK293 cells. Constructs were engineered with the M3- M4 intracellular domain replaced either by a GLVI linker sequence (SQPARAA) or by a modified GLVI sequence containing Escherichia coli cytochrome B562RIL41. The sample was prepared in the presence of GABA and nanobody a3NB77#1-#40RECOMBINANT
2GABA-A receptorCOMPLEX#1-#31RECOMBINANT
3Nanobody a3NB77COMPLEX#41RECOMBINANT
Source (natural)
IDEntity assembly-IDOrganismNcbi tax-ID
21Homo sapiens (human)9606
32Homo sapiens (human)9606
33Lama glama (llama)9844
Source (recombinant)
IDEntity assembly-IDOrganismNcbi tax-IDCellPlasmid
21Homo sapiens (human)9606
22Homo sapiens (human)9606Expi293F GnTI-pHLsec
33Homo sapiens (human)9606Expi293FpHLsec
Buffer solutionpH: 7.6
Details: 75 millimolar sodium chloride; 12.5 millimolar HEPES, pH 7.6; 1.5 millimolar 1D4 peptide
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Details: Nanodisc-reconstituted alpha3beta3gamma2 GABA-A receptor in complex with with GABA and nanobody a3NB77
Specimen supportGrid type: UltrAuFoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 95 % / Chamber temperature: 277 K

-
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: OTHER
Electron lensMode: BRIGHT FIELD / Nominal magnification: 130000 X / Nominal defocus max: 2200 nm / Nominal defocus min: 800 nm / Cs: 2.7 mm / C2 aperture diameter: 50 µm
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recording
IDImaging-IDElectron dose (e/Å2)Film or detector modelNum. of real images
1151.25GATAN K3 BIOQUANTUM (6k x 4k)3739
2151.25GATAN K3 BIOQUANTUM (6k x 4k)
3151.25GATAN K3 BIOQUANTUM (6k x 4k)

-
Processing

EM software
IDNameVersionCategoryImage processing-ID
1cryoSPARC4.4.1 to 4.7.1particle selection1
4cryoSPARC4.4.1 to 4.7.1CTF correction1
7UCSF Chimera1.8model fitting
9PHENIX1.20.1_4487model refinement
10cryoSPARC4.4.1 to 4.7.1initial Euler assignment1
11cryoSPARC4.4.1 to 4.7.1final Euler assignment1
13cryoSPARC4.4.1 to 4.7.13D reconstruction1
14cryoSPARC4.4.1 to 4.7.1particle selection2
19cryoSPARC4.4.1 to 4.7.13D reconstruction2
20cryoSPARC4.4.1 to 4.7.1particle selection3
21cryoSPARCparticle selection3
26cryoSPARC3D reconstruction3
27cryoSPARCparticle selection4
32cryoSPARC3D reconstruction4
33cryoSPARC4.4.1 to 4.7.1particle selection5
34cryoSPARC4.4.1 to 4.7.1CTF correction5
35cryoSPARC4.4.1 to 4.7.1initial Euler assignment5
36cryoSPARC4.4.1 to 4.7.1final Euler assignment5
38cryoSPARC4.4.1 to 4.7.13D reconstruction5
Image processing
IDImage recording-ID
11
22
33
41
51
CTF correction
IDEM image processing-IDType
11PHASE FLIPPING AND AMPLITUDE CORRECTION
22PHASE FLIPPING AND AMPLITUDE CORRECTION
33PHASE FLIPPING AND AMPLITUDE CORRECTION
44PHASE FLIPPING AND AMPLITUDE CORRECTION
55PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selection
IDImage processing-IDNum. of particles selected
11578387
21578387
31578387
42578387
52578387
62578387
73578387
83578387
93578387
104
114
124
135630021
145578387
155578387
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstruction
IDResolution (Å)Resolution methodNum. of particlesImage processing-IDEntry-IDSymmetry type
12.9FSC 0.143 CUT-OFF8939019TPQPOINT
22.94FSC 0.143 CUT-OFF8939019TPQPOINT
32.94FSC 0.143 CUT-OFF8939019TPQPOINT
42.94FSC 0.143 CUT-OFF8939019TPQPOINT
52.94FSC 0.143 CUT-OFF8939019TPQPOINT
62.9FSC 0.143 CUT-OFF8939029TPQPOINT
72.94FSC 0.143 CUT-OFF8939029TPQPOINT
82.94FSC 0.143 CUT-OFF8939029TPQPOINT
92.94FSC 0.143 CUT-OFF8939029TPQPOINT
102.94FSC 0.143 CUT-OFF8939029TPQPOINT
112.9FSC 0.143 CUT-OFF8939039TPQPOINT
122.94FSC 0.143 CUT-OFF8939039TPQPOINT
132.94FSC 0.143 CUT-OFF8939039TPQPOINT
142.94FSC 0.143 CUT-OFF8939039TPQPOINT
152.94FSC 0.143 CUT-OFF8939039TPQPOINT
162.9FSC 0.143 CUT-OFF8939049TPQPOINT
172.94FSC 0.143 CUT-OFF8939049TPQPOINT
182.94FSC 0.143 CUT-OFF8939049TPQPOINT
192.94FSC 0.143 CUT-OFF8939049TPQPOINT
202.94FSC 0.143 CUT-OFF8939049TPQPOINT
212.9FSC 0.143 CUT-OFF8939059TPQPOINT
222.94FSC 0.143 CUT-OFF8939059TPQPOINT
232.94FSC 0.143 CUT-OFF8939059TPQPOINT
242.94FSC 0.143 CUT-OFF8939059TPQPOINT
252.94FSC 0.143 CUT-OFF8939059TPQPOINT
RefinementHighest resolution: 2.9 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00316112
ELECTRON MICROSCOPYf_angle_d0.49421922
ELECTRON MICROSCOPYf_dihedral_angle_d4.712363
ELECTRON MICROSCOPYf_chiral_restr0.0572598
ELECTRON MICROSCOPYf_plane_restr0.0072665

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more