[English] 日本語
Yorodumi
- EMDB-46826: Focused region on azoRhuA-bCDRhuA co-assembled nanotubes -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-46826
TitleFocused region on azoRhuA-bCDRhuA co-assembled nanotubes
Map data
Sample
  • Complex: Helical assembly of azobenzene and beta-cyclodextrin modified RhuA
    • Protein or peptide: Rhamnulose-1-phosphate aldolase
  • Ligand: ZINC ION
  • Ligand: 1-[4-(2-phenylhydrazin-1-yl)phenyl]pyrrolidine-2,5-dione
KeywordsAssembly / LYASE
Function / homology
Function and homology information


rhamnulose-1-phosphate aldolase / rhamnulose-1-phosphate aldolase activity / rhamnose catabolic process / pentose catabolic process / aldehyde-lyase activity / metal ion binding / identical protein binding / cytosol
Similarity search - Function
Rhamnulose-1-phosphate aldolase / : / Class II aldolase/adducin N-terminal / Class II Aldolase and Adducin N-terminal domain / Class II Aldolase and Adducin N-terminal domain / Class II aldolase/adducin N-terminal domain superfamily
Similarity search - Domain/homology
Rhamnulose-1-phosphate aldolase
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.03 Å
AuthorsZhang Z / Sonani RR / Wang F / Egelman EH / Tezcan FA
Funding support United States, 1 items
OrganizationGrant numberCountry
Department of Energy (DOE, United States) United States
CitationJournal: Chem / Year: 2025
Title: Design of light-and chemically responsive protein assemblies through host-guest interactions
Authors: Zhang Z / Chiang HT / Xia Y / Avakyan N / Sonani RR / Wang F / Egelman EH / De Yoreo JJ / Pozzo LD / Tezcan FA
History
DepositionSep 2, 2024-
Header (metadata) releaseJul 16, 2025-
Map releaseJul 16, 2025-
UpdateJul 16, 2025-
Current statusJul 16, 2025Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_46826.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.86 Å/pix.
x 384 pix.
= 330.24 Å
0.86 Å/pix.
x 384 pix.
= 330.24 Å
0.86 Å/pix.
x 384 pix.
= 330.24 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.86 Å
Density
Contour LevelBy AUTHOR: 0.3
Minimum - Maximum-1.3709447 - 2.2194786
Average (Standard dev.)0.008683947 (±0.072585665)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 330.24 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Additional map: local filtered volume map

Fileemd_46826_additional_1.map
Annotationlocal filtered volume map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Additional map: EMready processed volume map

Fileemd_46826_additional_2.map
AnnotationEMready processed volume map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #1

Fileemd_46826_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #2

Fileemd_46826_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : Helical assembly of azobenzene and beta-cyclodextrin modified RhuA

EntireName: Helical assembly of azobenzene and beta-cyclodextrin modified RhuA
Components
  • Complex: Helical assembly of azobenzene and beta-cyclodextrin modified RhuA
    • Protein or peptide: Rhamnulose-1-phosphate aldolase
  • Ligand: ZINC ION
  • Ligand: 1-[4-(2-phenylhydrazin-1-yl)phenyl]pyrrolidine-2,5-dione

-
Supramolecule #1: Helical assembly of azobenzene and beta-cyclodextrin modified RhuA

SupramoleculeName: Helical assembly of azobenzene and beta-cyclodextrin modified RhuA
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Escherichia coli (E. coli)

-
Macromolecule #1: Rhamnulose-1-phosphate aldolase

MacromoleculeName: Rhamnulose-1-phosphate aldolase / type: protein_or_peptide / ID: 1 / Number of copies: 16 / Enantiomer: LEVO / EC number: rhamnulose-1-phosphate aldolase
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 30.088361 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MQNITQSWFV QGMIKATTDA WLKGWDERNG GNLTLRLDDA DIAPYHDNFH QQPRYIPLSQ PMPLLANTPF IVTGSGKFFR NVQLDPAAN LGIVKVDSCG AGYHILWGLT NEAVPTSELP AHFLSHSERI KATNGKDRVI MHCHATNLIA LTYVLENDTA V FTRQLWEG ...String:
MQNITQSWFV QGMIKATTDA WLKGWDERNG GNLTLRLDDA DIAPYHDNFH QQPRYIPLSQ PMPLLANTPF IVTGSGKFFR NVQLDPAAN LGIVKVDSCG AGYHILWGLT NEAVPTSELP AHFLSHSERI KATNGKDRVI MHCHATNLIA LTYVLENDTA V FTRQLWEG STECLVVFPD GVGILPWMVP GTDAIGQATA QEMQKHSLVL WPFHGVFGSG PTLDETFGLI DTAEKSAQVL VK VYSMGGM KQTISREELI ALGKRFGVTP LASALAL

UniProtKB: Rhamnulose-1-phosphate aldolase

-
Macromolecule #3: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 3 / Number of copies: 16 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

-
Macromolecule #4: 1-[4-(2-phenylhydrazin-1-yl)phenyl]pyrrolidine-2,5-dione

MacromoleculeName: 1-[4-(2-phenylhydrazin-1-yl)phenyl]pyrrolidine-2,5-dione
type: ligand / ID: 4 / Number of copies: 2 / Formula: A1A4G
Molecular weightTheoretical: 281.309 Da

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation statehelical array

-
Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / 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: 2.1 µm / Nominal defocus min: 1.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

CTF correctionSoftware - Name: cryoSPARC / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.03 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 440307
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
FSC plot (resolution estimation)

+
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