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- EMDB-63837: Structure of UBE3A T485E tetramer -

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Basic information

Entry
Database: EMDB / ID: EMD-63837
TitleStructure of UBE3A T485E tetramer
Map data
Sample
  • Complex: UBE3A T485E homo-tetramer
    • Protein or peptide: Isoform I of Ubiquitin-protein ligase E3A
KeywordsE3 Ligase / LIGASE
Function / homology
Function and homology information


regulation of ubiquitin-dependent protein catabolic process / Golgi lumen acidification / HECT-type E3 ubiquitin transferase / progesterone receptor signaling pathway / response to progesterone / postsynaptic cytosol / protein autoubiquitination / protein K48-linked ubiquitination / negative regulation of TORC1 signaling / positive regulation of protein ubiquitination ...regulation of ubiquitin-dependent protein catabolic process / Golgi lumen acidification / HECT-type E3 ubiquitin transferase / progesterone receptor signaling pathway / response to progesterone / postsynaptic cytosol / protein autoubiquitination / protein K48-linked ubiquitination / negative regulation of TORC1 signaling / positive regulation of protein ubiquitination / brain development / regulation of synaptic plasticity / regulation of circadian rhythm / protein polyubiquitination / ubiquitin-protein transferase activity / ubiquitin protein ligase activity / synaptic vesicle / Antigen processing: Ubiquitination & Proteasome degradation / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / transcription coactivator activity / glutamatergic synapse / proteolysis / nucleus / cytosol / cytoplasm
Similarity search - Function
Ubiquitin-protein ligase E3A / Ubiquitin-protein ligase E3A, N-terminal zinc-binding domain / Ubiquitin-protein ligase E3A, N-terminal zinc-binding domain superfamily / Amino-terminal Zinc-binding domain of ubiquitin ligase E3A / Ubiquitin-protein ligase E3B/C / HECT domain / HECT, E3 ligase catalytic domain / HECT-domain (ubiquitin-transferase) / HECT domain profile. / Domain Homologous to E6-AP Carboxyl Terminus with
Similarity search - Domain/homology
Ubiquitin-protein ligase E3A
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsRen XK / Xin J / Liu JB / Chen SW / Yan KG / Liu XT / Zhang MJ
Funding support China, 5 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)82188101 China
Other government2023B0303010001
Other government2021ZT09Y104
Other governmentKQTD20210811090115021
Other governmentA2303054
CitationJournal: To Be Published
Title: Structure of UBE3A T485E tetramer
Authors: Ren XK / Xin J / Liu JB / Chen SW / Yan KG / Liu XT / Zhang MJ
History
DepositionMar 19, 2025-
Header (metadata) releaseSep 23, 2026-
Map releaseSep 23, 2026-
UpdateSep 23, 2026-
Current statusSep 23, 2026Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_63837.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.66 Å/pix.
x 480 pix.
= 316.8 Å
0.66 Å/pix.
x 480 pix.
= 316.8 Å
0.66 Å/pix.
x 480 pix.
= 316.8 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.66 Å
Density
Contour LevelBy AUTHOR: 0.2
Minimum - Maximum-0.71280646 - 1.347146
Average (Standard dev.)-0.00058564375 (±0.032577887)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions480480480
Spacing480480480
CellA=B=C: 316.80002 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_63837_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #2

Fileemd_63837_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #1

Fileemd_63837_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : UBE3A T485E homo-tetramer

EntireName: UBE3A T485E homo-tetramer
Components
  • Complex: UBE3A T485E homo-tetramer
    • Protein or peptide: Isoform I of Ubiquitin-protein ligase E3A

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Supramolecule #1: UBE3A T485E homo-tetramer

SupramoleculeName: UBE3A T485E homo-tetramer / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Isoform I of Ubiquitin-protein ligase E3A

MacromoleculeName: Isoform I of Ubiquitin-protein ligase E3A / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO / EC number: HECT-type E3 ubiquitin transferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 98.413836 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: GPGSMKRAAA KHLIERYYHQ LTEGCGNEAC TNEFCASCPT FLRMDNNAAA IKALELYKIN AKLCDPHPSK KGASSAYLEN SKGAPNNSC SEIKMNKKGA RIDFKDVTYL TEEKVYEILE LCREREDYSP LIRVIGRVFS SAEALVQSFR KVKQHTKEEL K SLQAKDED ...String:
GPGSMKRAAA KHLIERYYHQ LTEGCGNEAC TNEFCASCPT FLRMDNNAAA IKALELYKIN AKLCDPHPSK KGASSAYLEN SKGAPNNSC SEIKMNKKGA RIDFKDVTYL TEEKVYEILE LCREREDYSP LIRVIGRVFS SAEALVQSFR KVKQHTKEEL K SLQAKDED KDEDEKEKAA CSAAAMEEDS EASSSRIGDS SQGDNNLQKL GPDDVSVDID AIRRVYTRLL SNEKIETAFL NA LVYLSPN VECDLTYHNV YSRDPNYLNL FIIVMENRNL HSPEYLEMAL PLFCKAMSKL PLAAQGKLIR LWSKYNADQI RRM METFQQ LITYKVISNE FNSRNLVNDD DAIVAASKCL KMVYYANVVG GEVDTNHNEE DDEEPIPESS ELTLQELLGE ERRN KKGPR VDPLETELGV KTLDCRKPLI PFEEFINEPL NEVLEMDKDY TFFKVETENK FSFMTCPFIL NAVTKNLGLY YDNRI RMYS ERRIEVLYSL VQGQQLNPYL RLKVRRDHII DDALVRLEMI AMENPADLKK QLYVEFEGEQ GVDEGGVSKE FFQLVV EEI FNPDIGMFTY DESTKLFWFN PSSFETEGQF TLIGIVLGLA IYNNCILDVH FPMVVYRKLM GKKGTFRDLG DSHPVLY QS LKDLLEYEGN VEDDMMITFQ ISQTDLFGNP MMYDLKENGD KIPITNENRK EFVNLYSDYI LNKSVEKQFK AFRRGFHM V TNESPLKYLF RPEEIELLIC GSRNLDFQAL EETTEYDGGY TRDSVLIREF WEIVHSFTDE QKRLFLQFTT GTDRAPVGG LGKLKMIIAK NGPDTERLPT SHTCFNVLLL PEYSSKEKLK ERLLKAITYA KGFGML

UniProtKB: Ubiquitin-protein ligase E3A

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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: 7.8
GridModel: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Average electron dose: 50.0 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: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING ONLY
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 137906
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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