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- EMDB-70670: Open state Gly/Glu/24S-HC bound hGluN1a-2B NMDAR -

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Basic information

Entry
Database: EMDB / ID: EMD-70670
TitleOpen state Gly/Glu/24S-HC bound hGluN1a-2B NMDAR
Map dataOpen state Gly/Glu/24S-HC bound hGluN1a-2B NMDAR - Composite map
Sample
  • Complex: Open-state GluN1-2B
    • Protein or peptide: Glutamate receptor ionotropic, NMDA 1
    • Protein or peptide: Glutamate receptor ionotropic, NMDA 2B
  • Ligand: GLYCINE
  • Ligand: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate
  • Ligand: GLUTAMIC ACID
  • Ligand: 24S-hydroxycholesterol
  • Ligand: water
KeywordsN-methyl-D-aspartate receptor / Open state / GluN2B / 24S-HC / MEMBRANE PROTEIN
Function / homology
Function and homology information


glycine-gated cation channel activity / excitatory chemical synaptic transmission / Activated NTRK2 signals through FYN / Synaptic adhesion-like molecules / response to glycine / propylene metabolic process / negative regulation of dendritic spine maintenance / Assembly and cell surface presentation of NMDA receptors / regulation of monoatomic cation transmembrane transport / NMDA glutamate receptor activity ...glycine-gated cation channel activity / excitatory chemical synaptic transmission / Activated NTRK2 signals through FYN / Synaptic adhesion-like molecules / response to glycine / propylene metabolic process / negative regulation of dendritic spine maintenance / Assembly and cell surface presentation of NMDA receptors / regulation of monoatomic cation transmembrane transport / NMDA glutamate receptor activity / Neurexins and neuroligins / NMDA selective glutamate receptor complex / glutamate binding / ligand-gated sodium channel activity / neurotransmitter receptor complex / glutamate receptor signaling pathway / calcium ion transmembrane import into cytosol / protein heterotetramerization / glycine binding / monoatomic cation transmembrane transport / positive regulation of reactive oxygen species biosynthetic process / Negative regulation of NMDA receptor-mediated neuronal transmission / Unblocking of NMDA receptors, glutamate binding and activation / positive regulation of calcium ion transport into cytosol / Long-term potentiation / excitatory synapse / monoatomic cation transport / monoatomic ion channel complex / regulation of neuronal synaptic plasticity / positive regulation of excitatory postsynaptic potential / synaptic cleft / positive regulation of synaptic transmission, glutamatergic / calcium ion homeostasis / MECP2 regulates neuronal receptors and channels / glutamate-gated calcium ion channel activity / EPHB-mediated forward signaling / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / ionotropic glutamate receptor signaling pathway / Ras activation upon Ca2+ influx through NMDA receptor / sodium ion transmembrane transport / synaptic membrane / regulation of membrane potential / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / synaptic transmission, glutamatergic / excitatory postsynaptic potential / postsynaptic density membrane / brain development / visual learning / regulation of synaptic plasticity / calcium ion transmembrane transport / long-term synaptic potentiation / terminal bouton / synaptic vesicle / late endosome / signaling receptor activity / amyloid-beta binding / RAF/MAP kinase cascade / response to ethanol / dendritic spine / chemical synaptic transmission / postsynaptic membrane / learning or memory / calmodulin binding / cytoskeleton / lysosome / neuron projection / postsynaptic density / calcium ion binding / synapse / dendrite / endoplasmic reticulum membrane / protein-containing complex binding / cell surface / positive regulation of transcription by RNA polymerase II / zinc ion binding / plasma membrane / cytoplasm
Similarity search - Function
Glutamate [NMDA] receptor, epsilon subunit, C-terminal / N-methyl D-aspartate receptor 2B3 C-terminus / : / : / Ionotropic glutamate receptor, metazoa / Ligated ion channel L-glutamate- and glycine-binding site / Ionotropic glutamate receptor, L-glutamate and glycine-binding domain / Ligated ion channel L-glutamate- and glycine-binding site / Ligand-gated ion channel / : ...Glutamate [NMDA] receptor, epsilon subunit, C-terminal / N-methyl D-aspartate receptor 2B3 C-terminus / : / : / Ionotropic glutamate receptor, metazoa / Ligated ion channel L-glutamate- and glycine-binding site / Ionotropic glutamate receptor, L-glutamate and glycine-binding domain / Ligated ion channel L-glutamate- and glycine-binding site / Ligand-gated ion channel / : / Ionotropic glutamate receptor / Eukaryotic homologues of bacterial periplasmic substrate binding proteins. / Receptor, ligand binding region / Receptor family ligand binding region / Periplasmic binding protein-like I
Similarity search - Domain/homology
Glutamate receptor ionotropic, NMDA 1 / Glutamate receptor ionotropic, NMDA 2B
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.15 Å
AuthorsHyunook K / Hiro F
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Mental Health (NIH/NIMH)MH085926 United States
National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)NS111745 United States
CitationJournal: Nature / Year: 2025
Title: Mechanism of conductance control and neurosteroid binding in NMDA receptors.
Authors: Hyunook Kang / Ruben Steigerwald / Elijah Z Ullman / Max Epstein / Srinu Paladugu / Dennis C Liotta / Stephen F Traynelis / Hiro Furukawa /
Abstract: Ion-channel activity reflects a combination of open probability and unitary conductance. Many channels display subconductance states that modulate signalling strength, yet the structural mechanisms ...Ion-channel activity reflects a combination of open probability and unitary conductance. Many channels display subconductance states that modulate signalling strength, yet the structural mechanisms governing conductance levels remain incompletely understood. Here we report that conductance levels are controlled by the bending patterns of pore-forming transmembrane helices in the heterotetrameric neuronal channel GluN1a-2B N-methyl-D-aspartate receptor (NMDAR). Our single-particle electron cryomicroscopy (cryo-EM) analyses demonstrate that an endogenous neurosteroid and synthetic positive allosteric modulator (PAM), 24S-hydroxycholesterol (24S-HC), binds to a juxtamembrane pocket in the GluN2B subunit and stabilizes the fully open-gate conformation, where GluN1a M3 and GluN2B M3' pore-forming helices are bent to dilate the channel pore. By contrast, EU1622-240 binds to the same GluN2B juxtamembrane pocket and a distinct juxtamembrane pocket in GluN1a to stabilize a sub-open state whereby only the GluN2B M3' helix is bent. Consistent with the varying extents of gate opening, the single-channel recordings predominantly show full-conductance and subconductance states in the presence of 24S-HC and EU1622-240, respectively. Another class of neurosteroid, pregnenolone sulfate, engages a similar GluN2B pocket, but two molecules bind simultaneously, revealing a diverse neurosteroid recognition pattern. Our study identifies that the juxtamembrane pockets are critical structural hubs for modulating conductance levels in NMDAR.
History
DepositionMay 16, 2025-
Header (metadata) releaseOct 29, 2025-
Map releaseOct 29, 2025-
UpdateDec 17, 2025-
Current statusDec 17, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_70670.png

Downloads & links

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Map

FileDownload / File: emd_70670.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationOpen state Gly/Glu/24S-HC bound hGluN1a-2B NMDAR - Composite map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 400 pix.
= 330.8 Å		0.83 Å/pix.
x 400 pix.
= 330.8 Å		0.83 Å/pix.
x 400 pix.
= 330.8 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.827 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.058
Minimum - Maximum-0.060719647 - 0.5881021
Average (Standard dev.)0.0022339486 (±0.010504138)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 330.80002 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Open-state GluN1-2B

EntireName: Open-state GluN1-2B
Components
  • Complex: Open-state GluN1-2B
    • Protein or peptide: Glutamate receptor ionotropic, NMDA 1
    • Protein or peptide: Glutamate receptor ionotropic, NMDA 2B
  • Ligand: GLYCINE
  • Ligand: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate
  • Ligand: GLUTAMIC ACID
  • Ligand: 24S-hydroxycholesterol
  • Ligand: water

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Supramolecule #1: Open-state GluN1-2B

SupramoleculeName: Open-state GluN1-2B / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 387 KDa

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Macromolecule #1: Glutamate receptor ionotropic, NMDA 1

MacromoleculeName: Glutamate receptor ionotropic, NMDA 1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 93.14932 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: ARAASDPKIV NIGAVLSTRK HEQMFREAVN QANKRHGSWK IQLNATSVTH KPNAIQMALS VCEDLISSQV YAILVSHPPT PNDHFTPTP VSYTAGFYRI PVLGLTTRMS IYSDKSIHLS FLRTVPPYSH QSSVWFEMMR VYSWNHIILL VSDDHEGRAA Q KRLETLLE ...String:
ARAASDPKIV NIGAVLSTRK HEQMFREAVN QANKRHGSWK IQLNATSVTH KPNAIQMALS VCEDLISSQV YAILVSHPPT PNDHFTPTP VSYTAGFYRI PVLGLTTRMS IYSDKSIHLS FLRTVPPYSH QSSVWFEMMR VYSWNHIILL VSDDHEGRAA Q KRLETLLE ERESKAEKVL QFDPGTKNVT ALLMEAKELE ARVIILSASE DDAATVYRAA AMLNMTGSGY VWLVGEREIS GN ALRYAPD GILGLQLING KNESAHISDA VGVVAQAVHE LLEKENITDP PRGCVGNTNI WKTGPLFKRV LMSSKYADGV TGR VEFNED GDRKFANYSI MNLQNRKLVQ VGIYNGTHVI PNDRKIIWPG GETEKPRGYQ MSTRLKIVTI HQEPFVYVKP TLSD GTCKE EFTVNGDPVK KVICTGPNDT SPGSPRHTVP QCCYGFCIDL LIKLARTMNF TYEVHLVADG KFGTQERVNN SNKKE WNGM MGELLSGQAD MIVAPLTINN ERAQYIEFSK PFKYQGLTIL VKKEIPRSTL DSFMQPFQST LWLLVGLSVH VVAVML YLL DRFSPFGRFK VNSEEEEEDA LTLSSAMWFS WGVLLNSGIG EGAPRSFSAR ILGMVWAGFA MIIVASYTAN LAAFLVL DR PEERITGIND PRLRNPSDKF IYATVKQSSV DIYFRRQVEL STMYRHMEKH NYESAAEAIQ AVRDNKLHAF IWDSAVLE F EASQKCDLVT TGELFFRSGF GIGMRKDSPW KQNVSLSILK SHENGFMEDL DKTWVRYQEC DSRSNAPATL TFENMAGVF MLVAGGIVAG IFLIFIEIAY KRHKDANGAQ

UniProtKB: Glutamate receptor ionotropic, NMDA 1

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Macromolecule #2: Glutamate receptor ionotropic, NMDA 2B

MacromoleculeName: Glutamate receptor ionotropic, NMDA 2B / type: protein_or_peptide / ID: 2 / Details: Twin-strep tag at the N-terminus / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 96.393797 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: WSHPQFEKGG GSGGGSGGSA WSHPQFEKGA LVPRGRSQKS PPSIGIAVIL VGTSDEVAIK DAHEKDDFHH LSVVPRVELV AMNETDPKS IITRICDLMS DRKIQGVVFA DDTDQEAIAQ ILDFISAQTL TPILGIHGGS SMIMADKDES SMFFQFGPSI E QQASVMLN ...String:
WSHPQFEKGG GSGGGSGGSA WSHPQFEKGA LVPRGRSQKS PPSIGIAVIL VGTSDEVAIK DAHEKDDFHH LSVVPRVELV AMNETDPKS IITRICDLMS DRKIQGVVFA DDTDQEAIAQ ILDFISAQTL TPILGIHGGS SMIMADKDES SMFFQFGPSI E QQASVMLN IMEEYDWYIF SIVTTYFPGY QDFVNKIRST IENSFVGWEL EEVLLLDMSL DDGDSKIQNQ LKKLQSPIIL LY CTKEEAT YIFEVANSVG LTGYGYTWIV PSLVAGDTDT VPAEFPTGLI SVSYDEWDYG LPARVRDGIA IITTAASDML SEH SFIPEP KSSCYNTHEK RIYQSNMLNR YLINVTFEGR NLSFSEDGYQ MHPKLVIILL NKERKWERVG KWKDKSLQMK YYVW PRMCP ETEEQEDDHL SIVTLEEAPF VIVESVDPLS GTCMRNTVPC QKRIVTENKT DEEPGYIKKC CKGFCIDILK KISKS VKFT YDLYLVTNGK HGKKINGTWN GMIGEVVMKR AYMAVGSLTI NEERSEVVDF SVPFIETGIS VMVSRSNGTV SPSAFL EPF SADVWVMMFV MLLIVSAVAV FVFEYFSPVG YNRSLADGRE PGGPSFTIGK AIWLLWGLVF NNSVPVQNPK GTTSKIM VS VWAFFAVIFL ASYTANLAAF MIQEEYVDQV SGLSDKKFQR PNDFSPPFRF GTVPNGSTER NIRNNYAEMH AYMGKFNQ R GVDDALLSLK TGKLDAFIYD AAVLNYMAGR DEGCKLVTIG SGKVFASTGY GIAIQKDSGW KRQVDLAILQ LFGDGEMEE LEALWLTGIC HNEKNEVMSS QLDIDNMAGV FYMLGAAMAL SLITFISEHL FYWQFRHSFM G

UniProtKB: Glutamate receptor ionotropic, NMDA 2B

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Macromolecule #3: GLYCINE

MacromoleculeName: GLYCINE / type: ligand / ID: 3 / Number of copies: 2 / Formula: GLY
Molecular weightTheoretical: 75.067 Da
Chemical component information

ChemComp-GLY:
GLYCINE

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Macromolecule #4: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(tri...

MacromoleculeName: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate
type: ligand / ID: 4 / Number of copies: 8 / Formula: POV
Molecular weightTheoretical: 760.076 Da
Chemical component information

ChemComp-POV:
(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipid*YM

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Macromolecule #5: GLUTAMIC ACID

MacromoleculeName: GLUTAMIC ACID / type: ligand / ID: 5 / Number of copies: 2 / Formula: GLU
Molecular weightTheoretical: 147.129 Da
Chemical component information

ChemComp-GLU:
GLUTAMIC ACID

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Macromolecule #6: 24S-hydroxycholesterol

MacromoleculeName: 24S-hydroxycholesterol / type: ligand / ID: 6 / Number of copies: 2 / Formula: A1CE1
Molecular weightTheoretical: 402.653 Da

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Macromolecule #7: water

MacromoleculeName: water / type: ligand / ID: 7 / Number of copies: 23 / 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

Concentration3 mg/mL
BufferpH: 8.5
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 200
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 281 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 14 eV
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 57.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 0.8 µm
Sample stageCooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 4468308
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER / Details: Ab initio reconstruction
Final reconstructionApplied symmetry - Point group: C2 (2 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.15 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 279700
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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Atomic model buiding 1

Initial model
PDB IDChain

9are

chain_id: A, source_name: PDB, initial_model_type: experimental model

9are

chain_id: B, source_name: PDB, initial_model_type: experimental model

9are

chain_id: C, source_name: PDB, initial_model_type: experimental model

9are

chain_id: D, source_name: PDB, initial_model_type: experimental model
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-9oor:
Open state Gly/Glu/24S-HC bound hGluN1a-2B NMDAR

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