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- EMDB-49888: Human delta 2 receptor in the resting state -

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ID or keywords:

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Basic information

Entry
Database: EMDB / ID: EMD-49888
TitleHuman delta 2 receptor in the resting state
Map dataWhole map locally sharpened
Sample
  • Complex: Human Delta-2 Receptor
    • Protein or peptide: Glutamate receptor ionotropic, delta-2
KeywordsLigand-gated ion channel / ion channel / neurotransmitter receptor / TRANSPORT PROTEIN
Function / homology
Function and homology information


trans-synaptic protein complex / cerebellar granule cell differentiation / positive regulation of long-term synaptic depression / excitatory synapse assembly / synaptic signaling via neuropeptide / regulation of postsynaptic density assembly / glutamate receptor activity / positive regulation of synapse assembly / heterophilic cell-cell adhesion / glutamate receptor signaling pathway ...trans-synaptic protein complex / cerebellar granule cell differentiation / positive regulation of long-term synaptic depression / excitatory synapse assembly / synaptic signaling via neuropeptide / regulation of postsynaptic density assembly / glutamate receptor activity / positive regulation of synapse assembly / heterophilic cell-cell adhesion / glutamate receptor signaling pathway / parallel fiber to Purkinje cell synapse / regulation of neuron projection development / AMPA glutamate receptor activity / regulation of neuron apoptotic process / AMPA glutamate receptor complex / ionotropic glutamate receptor complex / regulation of presynapse assembly / prepulse inhibition / regulation of postsynaptic membrane neurotransmitter receptor levels / excitatory postsynaptic potential / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / synaptic transmission, glutamatergic / PDZ domain binding / postsynaptic density membrane / modulation of chemical synaptic transmission / intracellular protein localization / scaffold protein binding / dendritic spine / synapse / glutamatergic synapse / metal ion binding / identical protein binding / plasma membrane
Similarity search - Function
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, delta-2
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.57 Å
AuthorsWang H / Ahmed F / Mondal AK / Twomey EC
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35GM154904 United States
CitationJournal: To Be Published
Title: Human Delta-2 receptors are ligand-gated ion channels
Authors: Wang H / Ahmed F / Mondal AK / Twomey EC
History
DepositionMar 24, 2025-
Header (metadata) releaseSep 24, 2025-
Map releaseSep 24, 2025-
UpdateSep 24, 2025-
Current statusSep 24, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_49888.map.gz / Format: CCP4 / Size: 343 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationWhole map locally sharpened
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.76 Å/pix.
x 448 pix.
= 340.48 Å
0.76 Å/pix.
x 448 pix.
= 340.48 Å
0.76 Å/pix.
x 448 pix.
= 340.48 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.76 Å
Density
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-0.5589709 - 0.98013943
Average (Standard dev.)0.0011903521 (±0.013135815)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions448448448
Spacing448448448
CellA=B=C: 340.47998 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: ECD local map locally sharpened

Fileemd_49888_additional_1.map
AnnotationECD local map locally sharpened
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Additional map: ECD local map half a

Fileemd_49888_additional_2.map
AnnotationECD local map half a
Projections & Slices
AxesZYX

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Slices (1/2)
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Additional map: ECD local map half b

Fileemd_49888_additional_3.map
AnnotationECD local map half b
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Additional map: TMD local map locally sharpened

Fileemd_49888_additional_4.map
AnnotationTMD local map locally sharpened
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Additional map: TMD local map half a

Fileemd_49888_additional_5.map
AnnotationTMD local map half a
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Additional map: TMD local map half b

Fileemd_49888_additional_6.map
AnnotationTMD local map half b
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: Whole map half a

Fileemd_49888_half_map_1.map
AnnotationWhole map half a
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: Whole map half b

Fileemd_49888_half_map_2.map
AnnotationWhole map half b
Projections & Slices
AxesZYX

Projections

Slices (1/2)
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Sample components

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Entire : Human Delta-2 Receptor

EntireName: Human Delta-2 Receptor
Components
  • Complex: Human Delta-2 Receptor
    • Protein or peptide: Glutamate receptor ionotropic, delta-2

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Supramolecule #1: Human Delta-2 Receptor

SupramoleculeName: Human Delta-2 Receptor / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Glutamate receptor ionotropic, delta-2

MacromoleculeName: Glutamate receptor ionotropic, delta-2 / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 94.287391 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: IHIGAIFDES AKKDDEVFRT AVGDLNQNEE ILQTEKITFS VTFVDGNNPF QAVQEACELM NQGILALVSS IGCTSAGSLQ SLADAMHIP HLFIQRSTAG TPRSGCGLTR SNRNDDYTLS VRPPVYLHDV ILRVVTEYAW QKFIIFYDSE YDIRGIQEFL D KVSQQGMD ...String:
IHIGAIFDES AKKDDEVFRT AVGDLNQNEE ILQTEKITFS VTFVDGNNPF QAVQEACELM NQGILALVSS IGCTSAGSLQ SLADAMHIP HLFIQRSTAG TPRSGCGLTR SNRNDDYTLS VRPPVYLHDV ILRVVTEYAW QKFIIFYDSE YDIRGIQEFL D KVSQQGMD VALQKVENNI NKMITTLFDT MRIEELNRYR DTLRRAILVM NPATAKSFIT EVVETNLVAF DCHWIIINEE IN DVDVQEL VRRSIGRLTI IRQTFPVPQN ISQRCFRGNH RISSTLCDPK DPFAQNMEIS NLYIYDTVLL LANAFHKKLE DRK WHSMAS LSCIRKNSKP WQGGRSMLET IKKGGVSGLT GELEFGENGG NPNVHFEILG TNYGEELGRG VRKLGCWNPV TGLN GSLTD KKLENNMRGV VLRVVTVLEE PFVMVSENVL GKPKKYQGFS IDVLDALSNY LGFNYEIYVA PDHKYGSPQE DGTWN GLVG ELVFKRADIG ISALTITPDR ENVVDFTTRY MDYSVGVLLR RAEKTVDMFA CLAPFDLSLW ACIAGTVLLV GLLVYL LNW LNPPRLQMGS MTSTTLYNSM WFVYGSFVQQ GGEVPYTTLA TRMMMGAWWL FALIVISSYT ANLAAFLTIT RIESSIQ SL QDLSKQTEIP YGTVLDSAVY EHVRMKGLNP FERDSMYSQM WRMINRSNGS ENNVLESQAG IQKVKYGNYA FVWDAAVL E YVAINDPDCS FYTIGNTVAD RGYGIALQHG SPYRDVFSQR ILELQQNGDM DILKHKWWPK NGQCDLYSSV DTKQKGGAL DIKSFAGVFC ILAAGIVLSC FIAMLETWWN KRKGSR

UniProtKB: Glutamate receptor ionotropic, delta-2

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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: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 45.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.9 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.57 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 87597
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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