[English] 日本語
Yorodumi
- EMDB-6859: Cryo-EM structure of L-fucokinase,GDP-fucose pyrophosphorylase (F... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-6859
TitleCryo-EM structure of L-fucokinase,GDP-fucose pyrophosphorylase (FKP) in Bacteroides fragilis
Map data
Sample
  • Complex: FKP
    • Protein or peptide: L-fucokinase, L-fucose-1-P guanylyltransferase
Keywordsbifunctional / kinase / ATP / GTP / TRANSFERASE
Function / homology
Function and homology information


nucleotidyltransferase activity / kinase activity / ATP binding
Similarity search - Function
L-fucokinase / L-fucokinase / Galactokinase/homoserine kinase / : / GHMP kinase, C-terminal domain / GHMP kinases C terminal / GHMP kinase N-terminal domain / GHMP kinases N terminal domain / GHMP kinase, C-terminal domain superfamily / Ribosomal protein S5 domain 2-type fold
Similarity search - Domain/homology
L-fucokinase/L-fucose-1-P guanylyltransferase
Similarity search - Component
Biological speciesBacteroides fragilis (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.2 Å
AuthorsWang J / Hu H
CitationJournal: Protein Cell / Year: 2019
Title: Cryo-EM structure of L-fucokinase/GDP-fucose pyrophosphorylase (FKP) in Bacteroides fragilis.
Authors: Ying Liu / Huifang Hu / Jia Wang / Qiang Zhou / Peng Wu / Nieng Yan / Hong-Wei Wang / Jia-Wei Wu / Linfeng Sun /
History
DepositionDec 11, 2017-
Header (metadata) releaseDec 12, 2018-
Map releaseDec 12, 2018-
UpdateMar 27, 2024-
Current statusMar 27, 2024Processing site: PDBj / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.017
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.017
  • Imaged by UCSF Chimera
  • Download
  • Surface view with fitted model
  • Atomic models: PDB-5yys
  • Surface level: 0.017
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_6859.map.gz / Format: CCP4 / Size: 52.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.3 Å/pix.
x 240 pix.
= 312. Å
1.3 Å/pix.
x 240 pix.
= 312. Å
1.3 Å/pix.
x 240 pix.
= 312. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.3 Å
Density
Contour LevelBy AUTHOR: 0.017 / Movie #1: 0.017
Minimum - Maximum-0.02450013 - 0.07406046
Average (Standard dev.)0.00037402968 (±0.0030467487)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions240240240
Spacing240240240
CellA=B=C: 312.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.31.31.3
M x/y/z240240240
origin x/y/z0.0000.0000.000
length x/y/z312.000312.000312.000
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ300300300
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS240240240
D min/max/mean-0.0250.0740.000

-
Supplemental data

-
Sample components

-
Entire : FKP

EntireName: FKP
Components
  • Complex: FKP
    • Protein or peptide: L-fucokinase, L-fucose-1-P guanylyltransferase

-
Supramolecule #1: FKP

SupramoleculeName: FKP / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Bacteroides fragilis (bacteria)

-
Macromolecule #1: L-fucokinase, L-fucose-1-P guanylyltransferase

MacromoleculeName: L-fucokinase, L-fucose-1-P guanylyltransferase / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Bacteroides fragilis (bacteria)
Molecular weightTheoretical: 105.782789 KDa
SequenceString: MQKLLSLPSN LVQSFHELER VNRTDWFCTS DPVGKKLGSG GGTSWLLEEC YNEYSDGATF GEWLEKEKRI LLHAGGQSRR LPGYAPSGK ILTPVPVFRW ERGQHLGQNL LSLQLPLYEK IMSLAPDKLH TLIASGDVYI RSEKPLQSIP EADVVCYGLW V DPSLATHH ...String:
MQKLLSLPSN LVQSFHELER VNRTDWFCTS DPVGKKLGSG GGTSWLLEEC YNEYSDGATF GEWLEKEKRI LLHAGGQSRR LPGYAPSGK ILTPVPVFRW ERGQHLGQNL LSLQLPLYEK IMSLAPDKLH TLIASGDVYI RSEKPLQSIP EADVVCYGLW V DPSLATHH GVFASDRKHP EQLDFMLQKP SLAELESLSK THLFLMDIGI WLLSDRAVEI LMKRSHKESS EELKYYDLYS DF GLALGTH PRIEDEEVNT LSVAILPLPG GEFYHYGTSK ELISSTLSVQ NKVYDQRRIM HRKVKPNPAM FVQNAVVRIP LCA ENADLW IENSHIGPKW KIASRHIITG VPENDWSLAV PAGVCVDVVP MGDKGFVARP YGLDDVFKGD LRDSKTTLTG IPFG EWMSK RGLSYTDLKG RTDDLQAVSV FPMVNSVEEL GLVLRWMLSE PELEEGKNIW LRSEHFSADE ISAGANLKRL YAQRE EFRK GNWKALAVNH EKSVFYQLDL ADAAEDFVRL GLDMPELLPE DALQMSRIHN RMLRARILKL DGKDYRPEEQ AAFDLL RDG LLDGISNRKS TPKLDVYSDQ IVWGRSPVRI DMAGGWTDTP PYSLYSGGNV VNLAIELNGQ PPLQVYVKPC KDFHIVL RS IDMGAMEIVS TFDELQDYKK IGSPFSIPKA ALSLAGFAPA FSAVSYASLE EQLKDFGAGI EVTLLAAIPA GSGLGTSS I LASTVLGAIN DFCGLAWDKN EICQRTLVLE QLLTTGGGWQ DQYGGVLQGV KLLQTEAGFA QSPLVRWLPD HLFTHPEYK DCHLLYYTGI TRTAKGILAE IVSSMFLNSS LHLNLLSEMK AHALDMNEAI QRGSFVEFGR LVGKTWEQNK ALDSGTNPPA VEAIIDLIK DYTLGYKLPG AGGGGYLYMV AKDPQAAVRI RKILTENAPN PRARFVEMTL SDKGFQVSRS

UniProtKB: L-fucokinase/L-fucose-1-P guanylyltransferase

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 8
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 400 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 120 sec.
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k 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
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 96749
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING
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