[English] 日本語
Yorodumi
- EMDB-64229: CryoEM structure of Brucella melitensis CobS dodecamer 2 without ... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-64229
TitleCryoEM structure of Brucella melitensis CobS dodecamer 2 without AMPPNP
Map data
Sample
  • Complex: CobS Dodecamer 2
    • Protein or peptide: Cobaltochelatase subunit CobS
KeywordsCobalt chelatase / CobS / AAA+ / ATPase / LIGASE
Function / homology
Function and homology information


cobaltochelatase / cobaltochelatase activity / cobalamin biosynthetic process / ATP hydrolysis activity / ATP binding
Similarity search - Function
Cobaltochelatase subunit CobS / Cobaltochelatase subunit CobS N-terminal domain / Cobaltochelatase CobS subunit N terminal / : / ATPase, dynein-related, AAA domain / AAA domain (dynein-related subfamily) / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Cobaltochelatase subunit CobS
Similarity search - Component
Biological speciesBrucella melitensis (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.02 Å
AuthorsZhou YL / Chen X / Liu L
Funding support China, 2 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)32471323 China
National Natural Science Foundation of China (NSFC)32371270 China
CitationJournal: Biorxiv / Year: 2026
Title: Assembly of the ATP-driven cobalt chelatase
Authors: Zhou YL / Yuan H / Wu YC / Wang J / Chen H / Yao L / Wang M / Wang X / Wang J / He C / Chen X / Liu L
History
DepositionApr 17, 2025-
Header (metadata) releaseJul 29, 2026-
Map releaseJul 29, 2026-
UpdateJul 29, 2026-
Current statusJul 29, 2026Processing site: PDBc / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_64229.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.7 Å/pix.
x 400 pix.
= 279.2 Å
0.7 Å/pix.
x 400 pix.
= 279.2 Å
0.7 Å/pix.
x 400 pix.
= 279.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.698 Å
Density
Contour LevelBy AUTHOR: 0.01
Minimum - Maximum-0.001672185 - 2.1098125
Average (Standard dev.)0.0031667321 (±0.041020658)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 279.2 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: #2

Fileemd_64229_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #1

Fileemd_64229_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : CobS Dodecamer 2

EntireName: CobS Dodecamer 2
Components
  • Complex: CobS Dodecamer 2
    • Protein or peptide: Cobaltochelatase subunit CobS

-
Supramolecule #1: CobS Dodecamer 2

SupramoleculeName: CobS Dodecamer 2 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Brucella melitensis (bacteria)

-
Macromolecule #1: Cobaltochelatase subunit CobS

MacromoleculeName: Cobaltochelatase subunit CobS / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO
Source (natural)Organism: Brucella melitensis (bacteria)
Molecular weightTheoretical: 36.768629 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MNKVERDIAN LPDTTVSVRE VFGIDSDMMV PAYAAGDSYV PELDPDYLFD RQTTLAILAG FAYNRRVMVS GYHGTGKSTH IEQVAARLN WPCVRVNLDS HVSRIDLVGK DAIVVKEGVQ VTEFKDGILP WAYQHNVALV FDEYDAGRPD VMFVIQRVLE S SGRLTLLD ...String:
MNKVERDIAN LPDTTVSVRE VFGIDSDMMV PAYAAGDSYV PELDPDYLFD RQTTLAILAG FAYNRRVMVS GYHGTGKSTH IEQVAARLN WPCVRVNLDS HVSRIDLVGK DAIVVKEGVQ VTEFKDGILP WAYQHNVALV FDEYDAGRPD VMFVIQRVLE S SGRLTLLD QSRVIRPHPA FRLFATANTV GLGDTTGLYH GTQQINQAQM DRWSIVTTLN YLPHDNEVNI VLVKAKHYQN AE GREIVNK MVRVADMTRQ AFINGDLSTV MSPRTVITWA ENAAIFNDVG FAFRLTFLNK CDELERATVA EFYQRAFGVE LPE SAANIV LA

UniProtKB: Cobaltochelatase subunit CobS

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation statefilament

-
Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeTFS GLACIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.4 µm

+
Image processing

Detailscryosparc
Particle selectionDetails: cryosparc
CTF correctionType: NONE
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.02 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 135929
Initial angle assignmentType: OTHER
Final angle assignmentType: COMMON LINE

+
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