[English] 日本語
Yorodumi
- PDB-7wff: Subcomplexes B,M and L in the Cylic electron transfer supercomple... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7wff
TitleSubcomplexes B,M and L in the Cylic electron transfer supercomplex NDH-PSI from Arabidopsis
Components
  • (NAD(P)H-quinone oxidoreductase subunit ...) x 6
  • (Photosynthetic NDH subunit of lumenal location ...) x 4
  • (Photosynthetic NDH subunit of subcomplex B ...) x 4
  • Isoform 2 of Photosynthetic NDH subunit of lumenal location 5, chloroplastic
  • NAD(P)H-quinone oxidoreductase chain 4, chloroplastic
  • NDH dependent flow 6
KeywordsELECTRON TRANSPORT / Subcomplex B / subcomplex M / subcomplex L / Arabidopisis / plant / cyclic electron transport supercomplex
Function / homology
Function and homology information


NAD(P)H dehydrogenase complex assembly / nitrite reductase complex [NAD(P)H] / NAD(P)H dehydrogenase complex (plastoquinone) / glucose-6-phosphate 1-epimerase activity / chloroplast stromal thylakoid / thylakoid lumen / protein histidine kinase binding / chloroplast membrane / P450-containing electron transport chain / chloroplast thylakoid ...NAD(P)H dehydrogenase complex assembly / nitrite reductase complex [NAD(P)H] / NAD(P)H dehydrogenase complex (plastoquinone) / glucose-6-phosphate 1-epimerase activity / chloroplast stromal thylakoid / thylakoid lumen / protein histidine kinase binding / chloroplast membrane / P450-containing electron transport chain / chloroplast thylakoid / ubiquinone biosynthetic process / NADPH dehydrogenase activity / thylakoid / Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions / chloroplast thylakoid lumen / photosystem II oxygen evolving complex / photosynthetic electron transport chain / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / oxidoreductase activity, acting on NAD(P)H / photosynthetic electron transport in photosystem I / plastid / cyclosporin A binding / extrinsic component of membrane / NADH dehydrogenase activity / photosynthesis, light reaction / electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity / chloroplast thylakoid membrane / electron transport coupled proton transport / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / protein peptidyl-prolyl isomerization / aerobic respiration / photosynthesis / chloroplast / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / electron transport chain / 2 iron, 2 sulfur cluster binding / protein folding / carbohydrate binding / response to oxidative stress / membrane => GO:0016020 / electron transfer activity / carbohydrate metabolic process / calcium ion binding / metal ion binding / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Photosynthetic NDH subunit of subcomplex B 4, chloroplastic / Photosynthetic NDH subunit of subcomplex B 1, chloroplastic / Photosynthetic NDH subunit of subcomplex B 5, chloroplastic / Photosynthetic NDH subunit of lumenal location 4-like / PsbP, C-terminal / PsbP / NADH:ubiquinone/plastoquinone oxidoreductase, chloroplast chain 5, C-terminal / NADH-dehyrogenase subunit F, TMs, (complex I) C-terminus / NADH-quinone oxidoreductase chain 4 / Oxygen-evolving enhancer protein 3 ...Photosynthetic NDH subunit of subcomplex B 4, chloroplastic / Photosynthetic NDH subunit of subcomplex B 1, chloroplastic / Photosynthetic NDH subunit of subcomplex B 5, chloroplastic / Photosynthetic NDH subunit of lumenal location 4-like / PsbP, C-terminal / PsbP / NADH:ubiquinone/plastoquinone oxidoreductase, chloroplast chain 5, C-terminal / NADH-dehyrogenase subunit F, TMs, (complex I) C-terminus / NADH-quinone oxidoreductase chain 4 / Oxygen-evolving enhancer protein 3 / Oxygen evolving enhancer protein 3 / NAD(P)H-quinone oxidoreductase subunit 2, N-terminal / NAD(P)H-quinone oxidoreductase subunit 2 N-terminal / Mog1/PsbP, alpha/beta/alpha sandwich / PsbQ-like domain superfamily / Adrenodoxin / NAD(P)H-quinone oxidoreductase subunit 3, bacterial/plastid / NAD(P)H-quinone oxidoreductase, subunit N/subunit 2 / Glycoside hydrolase-type carbohydrate-binding / 2Fe-2S iron-sulfur cluster binding domain / NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ / NADH-plastoquinone oxidoreductase, chain 5 subgroup / NADH-quinone oxidoreductase, chain M/4 / Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site / Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. / NADH-ubiquinone oxidoreductase chain 4L/K / NADH:ubiquinone/plastoquinone oxidoreductase, chain 6 / NADH-ubiquinone/plastoquinone oxidoreductase chain 6 / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminal / NADH-quinone oxidoreductase, chain 5-like / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus / NADH-ubiquinone oxidoreductase chain 4L/Mnh complex subunit C1-like / NADH-ubiquinone/plastoquinone oxidoreductase chain 4L / NADH:ubiquinone/plastoquinone oxidoreductase, chain 3 / NADH:ubiquinone oxidoreductase, subunit 3 superfamily / NADH-ubiquinone/plastoquinone oxidoreductase, chain 3 / NADH:ubiquinone oxidoreductase, subunit 1, conserved site / Respiratory-chain NADH dehydrogenase subunit 1 signature 1. / Respiratory-chain NADH dehydrogenase subunit 1 signature 2. / Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain profile. / NADH:ubiquinone oxidoreductase, subunit 1/F420H2 oxidoreductase subunit H / NADH dehydrogenase / Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain / Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD / NADH:ubiquinone oxidoreductase / NADH:quinone oxidoreductase/Mrp antiporter, membrane subunit / Proton-conducting membrane transporter / Cyclophilin-like domain superfamily / Galactose mutarotase-like domain superfamily / FKBP-type peptidyl-prolyl cis-trans isomerase domain profile. / FKBP-type peptidyl-prolyl cis-trans isomerase domain / FKBP-type peptidyl-prolyl cis-trans isomerase / Beta-grasp domain superfamily / Peptidyl-prolyl cis-trans isomerase domain superfamily / 2Fe-2S ferredoxin-type iron-sulfur binding domain / 2Fe-2S ferredoxin-like superfamily
Similarity search - Domain/homology
FE2/S2 (INORGANIC) CLUSTER / 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE / Chem-SQD / NAD(P)H-quinone oxidoreductase chain 4, chloroplastic / NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic / NDH dependent flow 6 / Photosynthetic NDH subunit of lumenal location 1, chloroplastic / NAD(P)H-quinone oxidoreductase subunit 4L, chloroplastic / NAD(P)H-quinone oxidoreductase subunit 3, chloroplastic / NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic ...FE2/S2 (INORGANIC) CLUSTER / 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE / Chem-SQD / NAD(P)H-quinone oxidoreductase chain 4, chloroplastic / NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic / NDH dependent flow 6 / Photosynthetic NDH subunit of lumenal location 1, chloroplastic / NAD(P)H-quinone oxidoreductase subunit 4L, chloroplastic / NAD(P)H-quinone oxidoreductase subunit 3, chloroplastic / NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic / NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic / Photosynthetic NDH subunit of subcomplex B 2, chloroplastic / NAD(P)H-quinone oxidoreductase subunit 6, chloroplastic / Photosynthetic NDH subunit of lumenal location 5, chloroplastic / Photosynthetic NDH subunit of subcomplex B 5, chloroplastic / Photosynthetic NDH subunit of subcomplex B 3, chloroplastic / Photosynthetic NDH subunit of subcomplex B 1, chloroplastic / Photosynthetic NDH subunit of lumenal location 4, chloroplastic / Photosynthetic NDH subunit of lumenal location 3, chloroplastic / Photosynthetic NDH subunit of lumenal location 2, chloroplastic
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.59 Å
AuthorsPan, X.W. / Li, M.
Funding support China, 5items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2017YFA0503702 China
Chinese Academy of SciencesXDB27020106 China
National Natural Science Foundation of China (NSFC)31770778 China
National Natural Science Foundation of China (NSFC)31930064 China
National Natural Science Foundation of China (NSFC)31970264 China
CitationJournal: Mol Plant / Year: 2022
Title: Supramolecular assembly of chloroplast NADH dehydrogenase-like complex with photosystem I from Arabidopsis thaliana.
Authors: Xiaodong Su / Duanfang Cao / Xiaowei Pan / Lifang Shi / Zhenfeng Liu / Luca Dall'Osto / Roberto Bassi / Xinzheng Zhang / Mei Li /
Abstract: Cyclic electron transport/flow (CET/CEF) in chloroplasts is a regulatory process essential for the optimization of plant photosynthetic efficiency. A crucial CEF pathway is catalyzed by a membrane- ...Cyclic electron transport/flow (CET/CEF) in chloroplasts is a regulatory process essential for the optimization of plant photosynthetic efficiency. A crucial CEF pathway is catalyzed by a membrane-embedded NADH dehydrogenase-like (NDH) complex that contains at least 29 protein subunits and associates with photosystem I (PSI) to form the NDH-PSI supercomplex. Here, we report the 3.9 Å resolution structure of the Arabidopsis thaliana NDH-PSI (AtNDH-PSI) supercomplex. We constructed structural models for 26 AtNDH subunits, among which 11 are unique to chloroplasts and stabilize the core part of the NDH complex. In the supercomplex, one NDH can bind up to two PSI-light-harvesting complex I (PSI-LHCI) complexes at both sides of its membrane arm. Two minor LHCIs, Lhca5 and Lhca6, each present in one PSI-LHCI, interact with NDH and contribute to supercomplex formation and stabilization. Collectively, our study reveals the structural details of the AtNDH-PSI supercomplex assembly and provides a molecular basis for further investigation of the regulatory mechanism of CEF in plants.
History
DepositionDec 26, 2021Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 16, 2022Provider: repository / Type: Initial release

-
Structure visualization

Movie
  • Deposited structure unit
  • Imaged by Jmol
  • Download
  • Simplified surface model + fitted atomic model
  • EMDB-32464
  • Imaged by Jmol
  • Download
  • Superimposition on EM map
  • EMDB-32464
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic
B: NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic
C: NAD(P)H-quinone oxidoreductase subunit 3, chloroplastic
D: NAD(P)H-quinone oxidoreductase chain 4, chloroplastic
E: NAD(P)H-quinone oxidoreductase subunit 4L, chloroplastic
F: NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic
G: NAD(P)H-quinone oxidoreductase subunit 6, chloroplastic
a: Photosynthetic NDH subunit of subcomplex B 1, chloroplastic
b: Photosynthetic NDH subunit of subcomplex B 2, chloroplastic
c: Photosynthetic NDH subunit of subcomplex B 3, chloroplastic
d: NDH dependent flow 6
e: Photosynthetic NDH subunit of subcomplex B 5, chloroplastic
f: Photosynthetic NDH subunit of lumenal location 1, chloroplastic
g: Photosynthetic NDH subunit of lumenal location 2, chloroplastic
h: Photosynthetic NDH subunit of lumenal location 3, chloroplastic
i: Photosynthetic NDH subunit of lumenal location 4, chloroplastic
j: Isoform 2 of Photosynthetic NDH subunit of lumenal location 5, chloroplastic
hetero molecules


Theoretical massNumber of molelcules
Total (without water)565,36821
Polymers562,95117
Non-polymers2,4174
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy
TypeNameSymmetry operationNumber
identity operation1_5551

-
Components

-
NAD(P)H-quinone oxidoreductase subunit ... , 6 types, 6 molecules ABCEFG

#1: Protein NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic / NAD(P)H dehydrogenase subunit 1 / NDH subunit 1 / NADH-plastoquinone oxidoreductase subunit 1


Mass: 40041.859 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress)
References: UniProt: Q37165, Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
#2: Protein NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic / NAD(P)H dehydrogenase / subunit 2 / NADH-plastoquinone oxidoreductase subunit 2


Mass: 57018.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress)
References: UniProt: A0A1B1W4Z4, Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
#3: Protein NAD(P)H-quinone oxidoreductase subunit 3, chloroplastic / NAD(P)H dehydrogenase subunit 3 / NADH-plastoquinone oxidoreductase subunit 3


Mass: 13846.332 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress)
References: UniProt: P56751, Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
#5: Protein NAD(P)H-quinone oxidoreductase subunit 4L, chloroplastic / NAD(P)H dehydrogenase subunit 4L / NADH-plastoquinone oxidoreductase subunit 4L


Mass: 11297.439 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress)
References: UniProt: P26289, Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
#6: Protein NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic / NAD(P)H dehydrogenase subunit 5 / NADH-plastoquinone oxidoreductase subunit 5


Mass: 85300.836 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress)
References: UniProt: P56752, Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
#7: Protein NAD(P)H-quinone oxidoreductase subunit 6, chloroplastic / NAD(P)H dehydrogenase subunit 6 / NADH-plastoquinone oxidoreductase subunit 6


Mass: 19218.639 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress)
References: UniProt: Q95695, Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions

-
Protein , 3 types, 3 molecules Ddj

#4: Protein NAD(P)H-quinone oxidoreductase chain 4, chloroplastic / NAD(P)H dehydrogenase / chain 4 / NADH-plastoquinone oxidoreductase chain 4


Mass: 56992.473 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress)
References: UniProt: A0A1B1W4Z0, Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
#11: Protein NDH dependent flow 6


Mass: 18699.324 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: B3H6Z4
#17: Protein Isoform 2 of Photosynthetic NDH subunit of lumenal location 5, chloroplastic / Cyclophilin of 20 kDa 2 / Peptidyl-prolyl cis-trans isomerase CYP20-2 / PPIase CYP20-2 / Rotamase ...Cyclophilin of 20 kDa 2 / Peptidyl-prolyl cis-trans isomerase CYP20-2 / PPIase CYP20-2 / Rotamase CYP20-2 / Thylakoid lumen PPIase of 20 kDa / TLP20


Mass: 27915.635 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9ASS6, peptidylprolyl isomerase

-
Photosynthetic NDH subunit of subcomplex B ... , 4 types, 4 molecules abce

#8: Protein Photosynthetic NDH subunit of subcomplex B 1, chloroplastic / Protein PnsB1 / NAD(P)H DEHYDROGENASE SUBUNIT 48 / NDH-DEPENDENT CYCLIC ELECTRON FLOW 1


Mass: 51080.168 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9S9N6
#9: Protein Photosynthetic NDH subunit of subcomplex B 2, chloroplastic / Protein PnsB2 / NAD(P)H DEHYDROGENASE SUBUNIT 45 / NDH-DEPENDENT CYCLIC ELECTRON FLOW 2


Mass: 38048.492 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q94AQ8
#10: Protein Photosynthetic NDH subunit of subcomplex B 3, chloroplastic / Protein PnsB3 / NDH-DEPENDENT CYCLIC ELECTRON FLOW 4


Mass: 22448.355 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9LU21
#12: Protein Photosynthetic NDH subunit of subcomplex B 5, chloroplastic / Protein PnsB5 / NAD(P)H dehydrogenase 18


Mass: 23767.838 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9FG89

-
Photosynthetic NDH subunit of lumenal location ... , 4 types, 4 molecules fghi

#13: Protein Photosynthetic NDH subunit of lumenal location 1, chloroplastic / PsbP-like protein 2


Mass: 26997.619 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: O80634
#14: Protein Photosynthetic NDH subunit of lumenal location 2, chloroplastic / PsbQ-like protein 1


Mass: 22183.342 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9XI73
#15: Protein Photosynthetic NDH subunit of lumenal location 3, chloroplastic / PsbQ-like protein 2


Mass: 24811.402 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9SGH4
#16: Protein Photosynthetic NDH subunit of lumenal location 4, chloroplastic / FK506-binding protein 16-2 / AtFKBP16-2 / Immunophilin FKBP16-2 / Peptidyl-prolyl cis-trans ...FK506-binding protein 16-2 / AtFKBP16-2 / Immunophilin FKBP16-2 / Peptidyl-prolyl cis-trans isomerase FKBP16-2 / PPIase FKBP16-2 / Rotamase


Mass: 23282.547 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9SCY3, peptidylprolyl isomerase

-
Non-polymers , 3 types, 4 molecules

#18: Chemical ChemComp-LHG / 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE / Phosphatidylglycerol


Mass: 722.970 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C38H75O10P / Comment: phospholipid*YM
#19: Chemical ChemComp-SQD / 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL / SULFOQUINOVOSYLDIACYLGLYCEROL


Mass: 795.116 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C41H78O12S
#20: Chemical ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster


Mass: 175.820 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe2S2 / Feature type: SUBJECT OF INVESTIGATION

-
Details

Has ligand of interestY

-
Experimental details

-
Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

-
Sample preparation

ComponentName: Cylic electron transfer supercomplex from Arabidopsis / Type: COMPLEX / Entity ID: #1-#17 / Source: NATURAL
Source (natural)Organism: Arabidopsis thaliana (thale cress)
Buffer solutionpH: 7.8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

-
Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2500 nm / Nominal defocus min: 1500 nm
Image recordingElectron dose: 60 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

-
Processing

SoftwareName: PHENIX / Version: 1.17.1_3660: / Classification: refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.59 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 136022 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00632900
ELECTRON MICROSCOPYf_angle_d0.89144616
ELECTRON MICROSCOPYf_dihedral_angle_d19.19611736
ELECTRON MICROSCOPYf_chiral_restr0.0485061
ELECTRON MICROSCOPYf_plane_restr0.0065530

+
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