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- PDB-9qef: Respiratory supercomplex from Mycobacterium smegmatis with decylu... -

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Basic information

Entry
Database: PDB / ID: 9qef
TitleRespiratory supercomplex from Mycobacterium smegmatis with decylubiquinone
Components
  • (Cytochrome bc1 complex cytochrome c ...) x 2
  • (Cytochrome c oxidase ...) x 3
  • Co-purified peptide
  • Co-purified transmembrane protein
  • Cytochrome bc1 complex cytochrome b subunit
  • LpqE protein
  • Probable cytochrome c oxidase subunit 3
  • Superoxide dismutase [Cu-Zn]
  • Transmembrane protein
  • Uncharacterized protein MSMEG_4692/MSMEI_4575
  • cytochrome-c oxidase
KeywordsELECTRON TRANSPORT / RESPIRATORY SUPERCOMPLEX / MEMBRANE PROTEIN / ACTINOBACTERIA
Function / homology
Function and homology information


aerobic electron transport chain / cytochrome-c oxidase / oxidative phosphorylation / quinol-cytochrome-c reductase / quinol-cytochrome-c reductase activity / cytochrome-c oxidase activity / superoxide dismutase / superoxide dismutase activity / electron transport coupled proton transport / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen ...aerobic electron transport chain / cytochrome-c oxidase / oxidative phosphorylation / quinol-cytochrome-c reductase / quinol-cytochrome-c reductase activity / cytochrome-c oxidase activity / superoxide dismutase / superoxide dismutase activity / electron transport coupled proton transport / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen / ATP synthesis coupled electron transport / respiratory electron transport chain / monooxygenase activity / electron transport chain / 2 iron, 2 sulfur cluster binding / iron ion binding / copper ion binding / heme binding / metal ion binding / membrane / plasma membrane
Similarity search - Function
Protein of unknown function DUF2631 / Protein of unknown function (DUF2631) / Protein of unknown function DUF5130 / Domain of unknown function (DUF5130) / Cytochrome bc1 complex, cytochrome c subunit / Cytochrome c oxidase subunit IV, actinobacteria / QcrA subunit, N-terminal / Cytochrome c oxidase subunit IV / QcrA subunit N-terminal region / Cytochrome b(N-terminal)/b6/petB ...Protein of unknown function DUF2631 / Protein of unknown function (DUF2631) / Protein of unknown function DUF5130 / Domain of unknown function (DUF5130) / Cytochrome bc1 complex, cytochrome c subunit / Cytochrome c oxidase subunit IV, actinobacteria / QcrA subunit, N-terminal / Cytochrome c oxidase subunit IV / QcrA subunit N-terminal region / Cytochrome b(N-terminal)/b6/petB / Cytochrome c oxidase, subunit I bacterial type / : / Cytochrome C oxidase, cbb3-type, subunit III / Cytochrome c oxidase subunit III / Cytochrome c oxidase subunit III-like / Cytochrome c oxidase, subunit III, 4-helical bundle / Cytochrome c oxidase subunit III / Heme-copper oxidase subunit III family profile. / Superoxide dismutase, copper/zinc, binding site / Copper/Zinc superoxide dismutase signature 2. / Cytochrome c oxidase subunit III-like superfamily / Superoxide dismutase, copper/zinc binding domain / Copper/zinc superoxide dismutase (SODC) / Superoxide dismutase-like, copper/zinc binding domain superfamily / Cytochrome c/quinol oxidase subunit II / Cytochrome C oxidase subunit II, transmembrane domain superfamily / Copper centre Cu(A) / CO II and nitrous oxide reductase dinuclear copper centers signature. / Cytochrome c oxidase, subunit I, copper-binding site / Heme-copper oxidase catalytic subunit, copper B binding region signature. / Cytochrome c oxidase-like, subunit I domain / Cytochrome oxidase subunit I profile. / Cytochrome c oxidase subunit I / Cytochrome c oxidase-like, subunit I superfamily / Cytochrome C and Quinol oxidase polypeptide I / Cytochrome C oxidase subunit II, periplasmic domain / Cytochrome c oxidase subunit II-like C-terminal / Cytochrome oxidase subunit II copper A binding domain profile. / Cytochrome c / Cytochrome b/b6, N-terminal / Cytochrome b/b6-like domain superfamily / Cytochrome b/b6 N-terminal region profile. / Di-haem cytochrome, transmembrane / Rieske iron-sulphur protein / Rieske [2Fe-2S] domain / Rieske [2Fe-2S] iron-sulphur domain / Rieske [2Fe-2S] iron-sulfur domain profile. / Rieske [2Fe-2S] iron-sulphur domain superfamily / Cytochrome c family profile. / Cytochrome c-like domain / Cytochrome c-like domain superfamily / Cupredoxin / Prokaryotic membrane lipoprotein lipid attachment site profile.
Similarity search - Domain/homology
1,2-Distearoyl-sn-glycerophosphoethanolamine / Chem-7PH / Chem-9XX / Chem-9YF / CARDIOLIPIN / COPPER (II) ION / Chem-DCQ / FE2/S2 (INORGANIC) CLUSTER / HEME-A / HEME C ...1,2-Distearoyl-sn-glycerophosphoethanolamine / Chem-7PH / Chem-9XX / Chem-9YF / CARDIOLIPIN / COPPER (II) ION / Chem-DCQ / FE2/S2 (INORGANIC) CLUSTER / HEME-A / HEME C / PROTOPORPHYRIN IX CONTAINING FE / Chem-IZL / MENAQUINONE-9 / PALMITIC ACID / TRIDECANE / : / Cytochrome c oxidase subunit 1 / Uncharacterized protein / Superoxide dismutase [Cu-Zn] / Transmembrane protein / Probable cytochrome c oxidase subunit 3 / Cytochrome bc1 complex cytochrome c subunit / Cytochrome bc1 complex Rieske iron-sulfur subunit / Cytochrome bc1 complex cytochrome b subunit / Cytochrome c oxidase polypeptide 4 / cytochrome-c oxidase / Uncharacterized protein MSMEG_4692/MSMEI_4575 / Uncharacterized protein / LpqE protein / Uncharacterized protein
Similarity search - Component
Biological speciesMycolicibacterium smegmatis (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.5 Å
AuthorsKovalova, T. / Krol, S. / Brzezinski, P. / Hogbom, M.
Funding support Sweden, 1items
OrganizationGrant numberCountry
Knut and Alice Wallenberg FoundationKAW 2019.0043 Sweden
CitationJournal: Commun Biol / Year: 2025
Title: Mycobacterial respiratory chain enzymes and growth are inhibited by decylubiquinone.
Authors: Sylwia Król / Terezia Kovalova / Mateusz Janczak / Sadaf Kalsum / Mira Akber / Martin Högbom / Susanna Brighenti / Pia Ädelroth / Peter Brzezinski /
Abstract: Aerobic organisms obtain energy by linking electron transfer from NADH to O, through the respiratory chain, to transmembrane proton translocation. In mycobacteria the respiratory chain is branched; ...Aerobic organisms obtain energy by linking electron transfer from NADH to O, through the respiratory chain, to transmembrane proton translocation. In mycobacteria the respiratory chain is branched; the membrane-bound electron carrier menaquinol (MQH) donates electrons either to the O-reducing cytochrome bd or a supercomplex that is composed of a complex (C) III dimer flanked by two CIVs. Here, we measured the dimethyl-naphthoquinone (DMNQH a menaquinol analogue) oxidation:O reduction activities of the CIIICIV supercomplex and cytochrome bd in the presence of an analogue (decylubiquinone, DCQ) of the mammalian electron carrier, ubiquinol. The data show that DCQH inhibits both the CIIICIV and cytochrome bd activities, suggesting that DCQ/DCQH interferes with both branches of the respiratory chain. Cryo-EM data of the M. smegmatis supercomplex shows that oxidized DCQ binds in the electron donor site (Q) of CIII. Accordingly, growth of M. smegmatis cells was impaired in the presence of DCQ. Remarkably, DCQ also impairs intracellular growth of virulent M. tuberculosis cells in human primary macrophages suggesting that the compound could potentially be used as an adjuvant during tuberculosis disease treatment.
History
DepositionMar 9, 2025Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 21, 2026Provider: repository / Type: Initial release
Revision 1.0Jan 21, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Jan 21, 2026Data content type: Additional map / Part number: 1 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0Jan 21, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jan 21, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jan 21, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Jan 21, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
O: Cytochrome bc1 complex cytochrome c subunit
M: Cytochrome bc1 complex cytochrome c subunit
N: Cytochrome bc1 complex cytochrome b subunit
P: Transmembrane protein
S: Probable cytochrome c oxidase subunit 3
T: Cytochrome c oxidase polypeptide 4
R: Cytochrome c oxidase subunit 1
Q: cytochrome-c oxidase
U: Cytochrome c oxidase subunit
V: Uncharacterized protein MSMEG_4692/MSMEI_4575
W: LpqE protein
Y: Superoxide dismutase [Cu-Zn]
C: Cytochrome bc1 complex cytochrome c subunit
G: Cytochrome bc1 complex cytochrome c subunit
H: Cytochrome bc1 complex cytochrome b subunit
I: Transmembrane protein
J: Probable cytochrome c oxidase subunit 3
K: Cytochrome c oxidase polypeptide 4
L: Cytochrome c oxidase subunit 1
X: cytochrome-c oxidase
Z: Cytochrome c oxidase subunit
a: Uncharacterized protein MSMEG_4692/MSMEI_4575
b: LpqE protein
c: Superoxide dismutase [Cu-Zn]
E: Co-purified transmembrane protein
F: Co-purified peptide
A: Co-purified transmembrane protein
B: Co-purified peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)808,261112
Polymers746,34028
Non-polymers61,92184
Water10,917606
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

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Cytochrome bc1 complex cytochrome c ... , 2 types, 4 molecules OCMG

#1: Protein Cytochrome bc1 complex cytochrome c subunit


Mass: 29109.945 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycolicibacterium smegmatis (bacteria) / Gene: MSMEG_4261 / Production host: Mycolicibacterium smegmatis (bacteria) / References: UniProt: A0R050, quinol-cytochrome-c reductase
#2: Protein Cytochrome bc1 complex cytochrome c subunit


Mass: 44869.395 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycolicibacterium smegmatis (bacteria) / Gene: MSMEG_4261 / Production host: Mycolicibacterium smegmatis (bacteria) / References: UniProt: A0R051, quinol-cytochrome-c reductase

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Protein , 9 types, 18 molecules NHPISJQXVaWbYcEAFB

#3: Protein Cytochrome bc1 complex cytochrome b subunit / Cytochrome bc1 reductase complex subunit QcrB


Mass: 61514.281 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycolicibacterium smegmatis (bacteria) / Gene: MSMEG_4263 / Production host: Mycolicibacterium smegmatis (bacteria) / References: UniProt: A0R052, quinol-cytochrome-c reductase
#4: Protein Transmembrane protein


Mass: 11329.909 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycolicibacterium smegmatis (bacteria) / Gene: MSMEG_2575 / Production host: Mycolicibacterium smegmatis (bacteria) / References: UniProt: A0QVH4
#5: Protein Probable cytochrome c oxidase subunit 3 / Cytochrome aa3 subunit 3


Mass: 22196.883 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycolicibacterium smegmatis (bacteria) / Gene: MSMEG_4260 / Production host: Mycolicibacterium smegmatis (bacteria) / References: UniProt: A0R049
#8: Protein cytochrome-c oxidase / Cytochrome aa3 subunit 2


Mass: 38077.465 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycolicibacterium smegmatis (bacteria) / Gene: MSMEG_4268 / Production host: Mycolicibacterium smegmatis (bacteria) / References: UniProt: A0R057, cytochrome-c oxidase
#10: Protein Uncharacterized protein MSMEG_4692/MSMEI_4575


Mass: 15910.971 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycolicibacterium smegmatis (bacteria) / Gene: MSMEG_4692, MSMEI_4575 / Production host: Mycolicibacterium smegmatis (bacteria) / References: UniProt: A0R1B5
#11: Protein LpqE protein


Mass: 19118.969 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycolicibacterium smegmatis (bacteria) / Gene: MSMEG_6078 / Production host: Mycolicibacterium smegmatis (bacteria) / References: UniProt: A0R562
#12: Protein Superoxide dismutase [Cu-Zn]


Mass: 23232.375 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycolicibacterium smegmatis (bacteria) / Gene: sodC, MSMEG_0835 / Production host: Mycolicibacterium smegmatis (bacteria) / References: UniProt: A0QQQ1, superoxide dismutase
#13: Protein Co-purified transmembrane protein


Mass: 13027.842 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycolicibacterium smegmatis (bacteria) / Gene: BIN_B_02039 / Production host: Mycolicibacterium smegmatis (bacteria) / References: UniProt: A0A653FDI6
#14: Protein Co-purified peptide


Mass: 7075.939 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycolicibacterium smegmatis (bacteria) / Gene: MSMEI_5553 / Production host: Mycolicibacterium smegmatis (bacteria) / References: UniProt: I7FT03

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Cytochrome c oxidase ... , 3 types, 6 molecules TKRLUZ

#6: Protein Cytochrome c oxidase polypeptide 4 / Cytochrome aa3 subunit 4 / Cytochrome c oxidase polypeptide IV


Mass: 15177.424 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycolicibacterium smegmatis (bacteria) / Gene: MSMEG_4267 / Production host: Mycolicibacterium smegmatis (bacteria) / References: UniProt: A0R056, cytochrome-c oxidase
#7: Protein Cytochrome c oxidase subunit 1


Mass: 64162.965 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycolicibacterium smegmatis (bacteria) / Gene: D806_022970 / Production host: Mycolicibacterium smegmatis (bacteria) / References: UniProt: A0A2U9PNL2, cytochrome-c oxidase
#9: Protein Cytochrome c oxidase subunit


Mass: 8365.549 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycolicibacterium smegmatis (bacteria) / Gene: MSMEG_4693 / Production host: Mycolicibacterium smegmatis (bacteria) / References: UniProt: A0R1B6

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Non-polymers , 19 types, 690 molecules

#15: Chemical
ChemComp-HEC / HEME C


Mass: 618.503 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H34FeN4O4
#16: Chemical
ChemComp-MQ9 / MENAQUINONE-9


Mass: 785.233 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C56H80O2
#17: Chemical
ChemComp-WUO / acyl-phosphatidyl-myo-inositol dimannoside (AcPIM2) / [(2R)-2-[(10E,13E)-hexadeca-10,13-dienoyl]oxy-3-[[(1S,2R,3R,4S,5S,6R)-2-[(2R,3S,4S,5S,6R)-6-(hexadecanoyloxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-6-[(2R,3S,4S,5S,6R)-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-3,4,5-tris(oxidanyl)cyclohexyl]oxy-oxidanyl-phosphoryl]oxy-propyl] (10R)-10-methyloctadecanoate / phosphatidylinositol mannoside


Mass: 1415.802 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C72H135O24P
#18: Chemical ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER


Mass: 175.820 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Fe2S2
#19: Chemical ChemComp-IZL / [(2~{R})-3-[[(1~{S},2~{R},3~{S},4~{S},5~{R},6~{R})-2-[(2~{R},3~{S},4~{S},5~{S},6~{R})-6-[[(2~{S},3~{S},4~{S},5~{S},6~{R})-6-[[(2~{S},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3-[(2~{R},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-4,5-bis(oxidanyl)oxan-2-yl]oxymethyl]-3,4,5-tris(oxidanyl)oxan-2-yl]oxymethyl]-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-3,4,5-tris(oxidanyl)-6-[(2~{R},3~{S},4~{S},5~{S},6~{R})-3,4,5-tris(oxidanyl)-6-(undecanoyloxymethyl)oxan-2-yl]oxy-cyclohexyl]oxy-oxidanyl-phosphoryl]oxy-2-undecanoyloxy-propyl] (10~{R})-10-methyldodecanoate


Mass: 1677.798 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C74H133O39P
#20: Chemical
ChemComp-9YF / (2R)-2-(hexadecanoyloxy)-3-{[(S)-hydroxy{[(1R,2R,3R,4R,5R,6S)-2,3,4,5,6-pentahydroxycyclohexyl]oxy}phosphoryl]oxy}propyl (9S)-9-methyloctadecanoate


Mass: 853.112 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C44H85O13P
#21: Chemical
ChemComp-7PH / (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate / PHOSPHATIDIC ACID


Mass: 564.732 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C29H57O8P
#22: Chemical
ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#23: Chemical
ChemComp-CDL / CARDIOLIPIN / DIPHOSPHATIDYL GLYCEROL / BIS-(1,2-DIACYL-SN-GLYCERO-3-PHOSPHO)-1',3'-SN-GLYCEROL


Mass: 1464.043 Da / Num. of mol.: 17 / Source method: obtained synthetically / Formula: C81H156O17P2 / Comment: phospholipid*YM
#24: Chemical
ChemComp-PLM / PALMITIC ACID


Mass: 256.424 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C16H32O2
#25: Chemical
ChemComp-9XX / (2S)-1-(hexadecanoyloxy)propan-2-yl (10S)-10-methyloctadecanoate / (S)-1-(palmitoyloxy)propan-2-yl (S)-10-methyloctadecanoate


Mass: 594.992 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C38H74O4
#26: Chemical
ChemComp-TRD / TRIDECANE / LIPID FRAGMENT


Mass: 184.361 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C13H28
#27: Chemical ChemComp-3PE / 1,2-Distearoyl-sn-glycerophosphoethanolamine / 3-SN-PHOSPHATIDYLETHANOLAMINE / 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE


Mass: 748.065 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C41H82NO8P / Comment: phospholipid*YM
#28: Chemical
ChemComp-HEA / HEME-A


Mass: 852.837 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C49H56FeN4O6
#29: Chemical
ChemComp-CU / COPPER (II) ION


Mass: 63.546 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Cu
#30: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#31: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#32: Chemical ChemComp-DCQ / 2-decyl-5,6-dimethoxy-3-methylcyclohexa-2,5-diene-1,4-dione / decylubiquinone


Mass: 322.439 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C19H30O4 / Feature type: SUBJECT OF INVESTIGATION
#33: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 606 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Has protein modificationY

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Experimental details

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Experiment

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

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Sample preparation

ComponentName: The respiratory supercomplex CIII2CIV2 / Type: COMPLEX / Entity ID: #1-#14 / Source: RECOMBINANT
Source (natural)Organism: Mycolicibacterium smegmatis (bacteria)
Source (recombinant)Organism: Mycolicibacterium smegmatis (bacteria)
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R2/2
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2200 nm / Nominal defocus min: 600 nm
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 40 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

EM softwareName: PHENIX / Version: 1.21.2_5419 / Category: model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 2.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 79 / Symmetry type: POINT
RefinementCross valid method: NONE
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
Displacement parametersBiso mean: 82.44 Å2
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.007549922
ELECTRON MICROSCOPYf_angle_d0.904567677
ELECTRON MICROSCOPYf_chiral_restr0.09477207
ELECTRON MICROSCOPYf_plane_restr0.00778255
ELECTRON MICROSCOPYf_dihedral_angle_d16.347118676

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