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- EMDB-4288: CryoEM structure of bovine cytochrome bc1 with no ligand bound -

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Basic information

Entry
Database: EMDB / ID: EMD-4288
TitleCryoEM structure of bovine cytochrome bc1 with no ligand bound
Map dataThe cryoEM map of bovine bc1 with no ligand bound.
Sample
  • Complex: Bovine cytochrome bc1 in the absence of any inhibitor.
    • Protein or peptide: x 10 types
  • Ligand: x 2 types
Function / homology
Function and homology information


mitochondrial respiratory chain complex III assembly / Respiratory electron transport / mitochondrial respiratory chain complex III / mitochondrial respiratory chain complex IV / quinol-cytochrome-c reductase / ubiquinone binding / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / respirasome / respiratory electron transport chain ...mitochondrial respiratory chain complex III assembly / Respiratory electron transport / mitochondrial respiratory chain complex III / mitochondrial respiratory chain complex IV / quinol-cytochrome-c reductase / ubiquinone binding / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / respirasome / respiratory electron transport chain / mitochondrial membrane / 2 iron, 2 sulfur cluster binding / metalloendopeptidase activity / mitochondrial inner membrane / oxidoreductase activity / heme binding / mitochondrion / proteolysis / membrane / metal ion binding
Similarity search - Function
Ubiquinol-cytochrome c reductase 8kDa, N-terminal / Ubiquinol-cytochrome c reductase 8 kDa, N-terminal / Globular protein, non-globular alpha/beta subunit / Cytochrome b-c1 complex, subunit 6 / Cytochrome b-c1 complex subunit 8 / UcrQ family / Cytochrome bc1 complex subunit Rieske, transmembrane domain superfamily / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 7 superfamily / Ubiquinol-cytochrome C reductase complex 14kD subunit ...Ubiquinol-cytochrome c reductase 8kDa, N-terminal / Ubiquinol-cytochrome c reductase 8 kDa, N-terminal / Globular protein, non-globular alpha/beta subunit / Cytochrome b-c1 complex, subunit 6 / Cytochrome b-c1 complex subunit 8 / UcrQ family / Cytochrome bc1 complex subunit Rieske, transmembrane domain superfamily / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 7 superfamily / Ubiquinol-cytochrome C reductase complex 14kD subunit / Cytochrome b-c1 complex subunit 9 / Cytochrome b-c1 complex subunit 8 superfamily / Cytochrome b-c1 complex subunit 9 superfamily / Ubiquinol-cytochrome C reductase, UQCRX/QCR9 like / Cytochrome b-c1 complex subunit Rieske, transmembrane domain / Ubiquinol cytochrome reductase transmembrane region / Ubiquinol-cytochrome C reductase hinge domain / Ubiquinol-cytochrome C reductase hinge domain superfamily / Ubiquinol-cytochrome C reductase hinge protein / Cytochrome c1, transmembrane anchor, C-terminal / Cytochrome b / : / : / Ubiquinol-cytochrome c reductase, iron-sulphur subunit / Cytochrome c1 / Cytochrome C1 family / Cytochrome b/b6, C-terminal / Cytochrome b(C-terminal)/b6/petD / Cytochrome b/b6 C-terminal region profile. / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / Rieske iron-sulphur protein, C-terminal / 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 / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / Metalloenzyme, LuxS/M16 peptidase-like / Rieske [2Fe-2S] iron-sulphur domain / Rieske [2Fe-2S] 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
Similarity search - Domain/homology
Cytochrome c1, heme protein, mitochondrial / Cytochrome b-c1 complex subunit 6, mitochondrial / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 9 / Cytochrome b / Cytochrome b-c1 complex subunit 8 / Cytochrome b-c1 complex subunit Rieske, mitochondrial / Cytochrome b-c1 complex subunit 2, mitochondrial / Cytochrome b-c1 complex subunit 1, mitochondrial
Similarity search - Component
Biological speciesBos taurus (cattle) / Bovine (cattle)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.4 Å
AuthorsJohnson RM / Amporndanai K / O'Neill PM / Fishwick CWG / Jamson AH / Rawson SD / Hasnain SS / Antonyuk SV / Muench SP
Funding support United Kingdom, 1 items
OrganizationGrant numberCountry
Wellcome Trust109158/B/15/Z United Kingdom
CitationJournal: IUCrJ / Year: 2018
Title: X-ray and cryo-EM structures of inhibitor-bound cytochrome complexes for structure-based drug discovery.
Authors: Kangsa Amporndanai / Rachel M Johnson / Paul M O'Neill / Colin W G Fishwick / Alexander H Jamson / Shaun Rawson / Stephen P Muench / S Samar Hasnain / Svetlana V Antonyuk /
Abstract: Cytochrome , a dimeric multi-subunit electron-transport protein embedded in the inner mitochondrial membrane, is a major drug target for the treatment and prevention of malaria and toxoplasmosis. ...Cytochrome , a dimeric multi-subunit electron-transport protein embedded in the inner mitochondrial membrane, is a major drug target for the treatment and prevention of malaria and toxoplasmosis. Structural studies of cytochrome from mammalian homologues co-crystallized with lead compounds have underpinned structure-based drug design to develop compounds with higher potency and selectivity. However, owing to the limited amount of cytochrome that may be available from parasites, all efforts have been focused on homologous cytochrome complexes from mammalian species, which has resulted in the failure of some drug candidates owing to toxicity in the host. Crystallographic studies of the native parasite proteins are not feasible owing to limited availability of the proteins. Here, it is demonstrated that cytochrome is highly amenable to single-particle cryo-EM (which uses significantly less protein) by solving the apo and two inhibitor-bound structures to ∼4.1 Å resolution, revealing clear inhibitor density at the binding site. Therefore, cryo-EM is proposed as a viable alternative method for structure-based drug discovery using both host and parasite enzymes.
History
DepositionFeb 5, 2018-
Header (metadata) releaseFeb 28, 2018-
Map releaseFeb 28, 2018-
UpdateDec 11, 2019-
Current statusDec 11, 2019Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.0548
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.0548
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6fo2
  • Surface level: 0.0548
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_4288.png

Downloads & links

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Map

FileDownload / File: emd_4288.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationThe cryoEM map of bovine bc1 with no ligand bound.
Voxel sizeX=Y=Z: 1.047 Å
Density
Contour LevelBy AUTHOR: 0.0548 / Movie #1: 0.0548
Minimum - Maximum-0.11153071 - 0.23522417
Average (Standard dev.)0.0040607345 (±0.014114776)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions200200200
Spacing200200200
CellA=B=C: 209.40001 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0471.0471.047
M x/y/z200200200
origin x/y/z0.0000.0000.000
length x/y/z209.400209.400209.400
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS200200200
D min/max/mean-0.1120.2350.004

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Supplemental data

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Additional map: The unsharpened map of apo-bc1.

Fileemd_4288_additional.map
AnnotationThe unsharpened map of apo-bc1.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: The first half map of apo-bc1.

Fileemd_4288_half_map_1.map
AnnotationThe first half map of apo-bc1.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: The second half map of apo-bc1.

Fileemd_4288_half_map_2.map
AnnotationThe second half map of apo-bc1.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Bovine cytochrome bc1 in the absence of any inhibitor.

EntireName: Bovine cytochrome bc1 in the absence of any inhibitor.
Components
  • Complex: Bovine cytochrome bc1 in the absence of any inhibitor.
    • Protein or peptide: Cytochrome b-c1 complex subunit 1, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 2, mitochondrial
    • Protein or peptide: Cytochrome b
    • Protein or peptide: Cytochrome c1, heme protein, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit Rieske, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 7
    • Protein or peptide: Cytochrome b-c1 complex subunit 8
    • Protein or peptide: Cytochrome b-c1 complex subunit 6, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit Rieske, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 9
  • Ligand: PROTOPORPHYRIN IX CONTAINING FE
  • Ligand: HEME C

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Supramolecule #1: Bovine cytochrome bc1 in the absence of any inhibitor.

SupramoleculeName: Bovine cytochrome bc1 in the absence of any inhibitor.
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#10
Source (natural)Organism: Bos taurus (cattle) / Organ: Heart / Location in cell: Mitochondria
Molecular weightExperimental: 480 KDa

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Macromolecule #1: Cytochrome b-c1 complex subunit 1, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 1, mitochondrial / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bovine (cattle)
Molecular weightTheoretical: 52.79641 KDa
SequenceString: MAASAVCRAA GAGTRVLLRT RRSPALLRSS DLRGTATYAQ ALQSVPETQV SQLDNGLRVA SEQSSQPTCT VGVWIDAGSR YESEKNNGA GYFVEHLAFK GTKNRPGNAL EKEVESMGAH LNAYSTREHT AYYIKALSKD LPKAVELLAD IVQNCSLEDS Q IEKERDVI ...String:
MAASAVCRAA GAGTRVLLRT RRSPALLRSS DLRGTATYAQ ALQSVPETQV SQLDNGLRVA SEQSSQPTCT VGVWIDAGSR YESEKNNGA GYFVEHLAFK GTKNRPGNAL EKEVESMGAH LNAYSTREHT AYYIKALSKD LPKAVELLAD IVQNCSLEDS Q IEKERDVI LQELQENDTS MRDVVFNYLH ATAFQGTPLA QSVEGPSENV RKLSRADLTE YLSRHYKAPR MVLAAAGGLE HR QLLDLAQ KHFSGLSGTY DEDAVPTLSP CRFTGSQICH REDGLPLAHV AIAVEGPGWA HPDNVALQVA NAIIGHYDCT YGG GAHLSS PLASIAATNK LCQSFQTFNI CYADTGLLGA HFVCDHMSID DMMFVLQGQW MRLCTSATES EVLRGKNLLR NALV SHLDG TTPVCEDIGR SLLTYGRRIP LAEWESRIAE VDARVVREVC SKYFYDQCPA VAGFGPIEQL PDYNRIRSGM FWLRF

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Macromolecule #2: Cytochrome b-c1 complex subunit 2, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 2, mitochondrial / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bovine (cattle)
Molecular weightTheoretical: 48.204418 KDa
SequenceString: MKLLTRAGSL SRFYSLKVAP KVKATEAPAG VPPHPQDLEF TRLPNGLVIA SLENYAPASR IGLFIKAGSR YENSNNLGTS HLLRLASSL TTKGASSFKI TRGIEAVGGK LSVTSTRENM AYTVECLRDD VDILMEFLLN VTTAPEFRRW EVAALQPQLR I DKAVALQN ...String:
MKLLTRAGSL SRFYSLKVAP KVKATEAPAG VPPHPQDLEF TRLPNGLVIA SLENYAPASR IGLFIKAGSR YENSNNLGTS HLLRLASSL TTKGASSFKI TRGIEAVGGK LSVTSTRENM AYTVECLRDD VDILMEFLLN VTTAPEFRRW EVAALQPQLR I DKAVALQN PQAHVIENLH AAAYRNALAN SLYCPDYRIG KVTPVELHDY VQNHFTSARM ALIGLGVSHP VLKQVAEQFL NI RGGLGLS GAKAKYHGGE IREQNGDSLV HAALVAESAA IGSAEANAFS VLQHVLGAGP HVKRGSNATS SLYQAVAKGV HEP FDVSAF NASYSDSGLF GFYTISQAAS AGDVIKAAYN QVKTIAQGNL SNPDVQAAKN KLKAGYLMSV ESSEGFLDEV GSQA LAAGS YTPPSTVLQQ IDAVADADVI NAAKKFVSGR KSMAASGNLG HTPFIDEL

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Macromolecule #3: Cytochrome b

MacromoleculeName: Cytochrome b / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bovine (cattle)
Molecular weightTheoretical: 42.62034 KDa
SequenceString: MTNIRKSHPL MKIVNNAFID LPAPSNISSW WNFGSLLGIC LILQILTGLF LAMHYTSDTT TAFSSVTHIC RDVNYGWIIR YMHANGASM FFICLYMHVG RGLYYGSYTF LETWNIGVIL LLTVMATAFM GYVLPWGQMS FWGATVITNL LSAIPYIGTN L VEWIWGGF ...String:
MTNIRKSHPL MKIVNNAFID LPAPSNISSW WNFGSLLGIC LILQILTGLF LAMHYTSDTT TAFSSVTHIC RDVNYGWIIR YMHANGASM FFICLYMHVG RGLYYGSYTF LETWNIGVIL LLTVMATAFM GYVLPWGQMS FWGATVITNL LSAIPYIGTN L VEWIWGGF SVDKATLTRF FAFHFILPFI IMAIAMVHLL FLHETGSNNP TGISSDVDKI PFHPYYTIKD ILGALLLILA LM LLVLFAP DLLGDPDNYT PANPLNTPPH IKPEWYFLFA YAILRSIPNK LGGVLALAFS ILILALIPLL HTSKQRSMMF RPL SQCLFW ALVADLLTLT WIGGQPVEHP YITIGQLASV LYFLLILVLM PTAGTIENKL LKW

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Macromolecule #4: Cytochrome c1, heme protein, mitochondrial

MacromoleculeName: Cytochrome c1, heme protein, mitochondrial / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bovine (cattle)
Molecular weightTheoretical: 35.34377 KDa
SequenceString: MAAAAATLRG AMVGPRGAGL PGARARGLLC GARPGQLPLR TPQAVSLSSK SGLSRGRKVI LSALGMLAAG GAGLAVALHS AVSASDLEL HPPSYPWSHR GLLSSLDHTS IRRGFQVYKQ VCSSCHSMDY VAYRHLVGVC YTEDEAKALA EEVEVQDGPN E DGEMFMRP ...String:
MAAAAATLRG AMVGPRGAGL PGARARGLLC GARPGQLPLR TPQAVSLSSK SGLSRGRKVI LSALGMLAAG GAGLAVALHS AVSASDLEL HPPSYPWSHR GLLSSLDHTS IRRGFQVYKQ VCSSCHSMDY VAYRHLVGVC YTEDEAKALA EEVEVQDGPN E DGEMFMRP GKLSDYFPKP YPNPEAARAA NNGALPPDLS YIVRARHGGE DYVFSLLTGY CEPPTGVSLR EGLYFNPYFP GQ AIGMAPP IYNEVLEFDD GTPATMSQVA KDVCTFLRWA AEPEHDHRKR MGLKMLLMMG LLLPLVYAMK RHKWSVLKSR KLA YRPPK

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Macromolecule #5: Cytochrome b-c1 complex subunit Rieske, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit Rieske, mitochondrial / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO / EC number: quinol-cytochrome-c reductase
Source (natural)Organism: Bovine (cattle)
Molecular weightTheoretical: 29.586842 KDa
SequenceString: MLSVAARSGP FAPVLSATSR GVAGALRPLV QAAVPATSES PVLDLKRSVL CRESLRGQAA GRPLVASVSL NVPASVRYSH TDIKVPDFS DYRRPEVLDS TKSSKESSEA RKGFSYLVTA TTTVGVAYAA KNVVSQFVSS MSASADVLAM SKIEIKLSDI P EGKNMAFK ...String:
MLSVAARSGP FAPVLSATSR GVAGALRPLV QAAVPATSES PVLDLKRSVL CRESLRGQAA GRPLVASVSL NVPASVRYSH TDIKVPDFS DYRRPEVLDS TKSSKESSEA RKGFSYLVTA TTTVGVAYAA KNVVSQFVSS MSASADVLAM SKIEIKLSDI P EGKNMAFK WRGKPLFVRH RTKKEIDQEA AVEVSQLRDP QHDLERVKKP EWVILIGVCT HLGCVPIANA GDFGGYYCPC HG SHYDASG RIRKGPAPLN LEVPSYEFTS DDMVIVG

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Macromolecule #6: Cytochrome b-c1 complex subunit 7

MacromoleculeName: Cytochrome b-c1 complex subunit 7 / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bovine (cattle)
Molecular weightTheoretical: 13.502387 KDa
SequenceString:
MAGRPAVSAS SRWLEGIRKW YYNAAGFNKL GLMRDDTIHE NDDVKEAIRR LPENLYDDRV FRIKRALDLS MRQQILPKEQ WTKYEEDKS YLEPYLKEVI RERKEREEWA KK

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Macromolecule #7: Cytochrome b-c1 complex subunit 8

MacromoleculeName: Cytochrome b-c1 complex subunit 8 / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bovine (cattle)
Molecular weightTheoretical: 9.737223 KDa
SequenceString:
MGRQFGHLTR VRHVITYSLS PFEQRAFPHY FSKGIPNVLR RTRACILRVA PPFVAFYLVY TWGTQEFEKS KRKNPAAYEN DR

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Macromolecule #8: Cytochrome b-c1 complex subunit 6, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 6, mitochondrial / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bovine (cattle)
Molecular weightTheoretical: 10.638744 KDa
SequenceString:
MGLEDEQRML TGSGDPKEEE EEEEELVDPL TTVREQCEQL EKCVKARERL ELCDERVSSR SQTEEDCTEE LLDFLHARDH CVAHKLFNS LK

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Macromolecule #9: Cytochrome b-c1 complex subunit Rieske, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit Rieske, mitochondrial / type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO / EC number: quinol-cytochrome-c reductase
Source (natural)Organism: Bovine (cattle)
Molecular weightTheoretical: 1.652936 KDa
SequenceString:
RPVVASVSLN VPASVR

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Macromolecule #10: Cytochrome b-c1 complex subunit 9

MacromoleculeName: Cytochrome b-c1 complex subunit 9 / type: protein_or_peptide / ID: 10 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bovine (cattle)
Molecular weightTheoretical: 7.469621 KDa
SequenceString:
MVAPTLTARL YSLLFRRTST FALTIVVGAL FFERAFDQGA DAIYEHINEG KLWKHIKHKY ENKE

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Macromolecule #11: PROTOPORPHYRIN IX CONTAINING FE

MacromoleculeName: PROTOPORPHYRIN IX CONTAINING FE / type: ligand / ID: 11 / Number of copies: 4 / Formula: HEM
Molecular weightTheoretical: 616.487 Da
Chemical component information

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE / Heme B

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Macromolecule #12: HEME C

MacromoleculeName: HEME C / type: ligand / ID: 12 / Number of copies: 2 / Formula: HEC
Molecular weightTheoretical: 618.503 Da
Chemical component information

ChemComp-HEC:
HEME C / Heme C

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration5.0 mg/mL
BufferpH: 7.5
Component:
ConcentrationNameFormula
25.0 mMTris-HClTris
100.0 mMSodium chlorideNaClSodium chloride
0.5 mMEDTAEthylenediaminetetraacetic acid
0.015 %DDM
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV
Details: blot for 6 seconds with a blot force of 6 before plunge-freezing.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 4.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 79000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Number real images: 3256 / Average exposure time: 12.0 sec. / Average electron dose: 44.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 260201
CTF correctionSoftware - Name: Gctf
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

5d6u


Details: The pdb file of an existing crystal structure was back-filtered to 60 A.
Initial angle assignmentType: PROJECTION MATCHING / Software - Name: RELION (ver. 2.0)
Final angle assignmentType: PROJECTION MATCHING / Software - Name: RELION (ver. 2.0)
Final reconstructionApplied symmetry - Point group: C2 (2 fold cyclic) / Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 4.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 2.0) / Number images used: 57571
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-6fo2:
CryoEM structure of bovine cytochrome bc1 with no ligand bound

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