[English] 日本語
Yorodumi
- EMDB-31883: Matrix arm of deactive state CI from DQ-NADH dataset -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-31883
TitleMatrix arm of deactive state CI from DQ-NADH dataset
Map data
Sample
  • Complex: Respiratory complex I
    • Protein or peptide: x 18 types
  • Ligand: x 12 types
Function / homology
Function and homology information


RHOG GTPase cycle / Complex I biogenesis / Respiratory electron transport / cardiac muscle tissue development / oxidoreductase activity, acting on NAD(P)H / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / electron transport chain ...RHOG GTPase cycle / Complex I biogenesis / Respiratory electron transport / cardiac muscle tissue development / oxidoreductase activity, acting on NAD(P)H / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / electron transport chain / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / negative regulation of intrinsic apoptotic signaling pathway / respirasome / reactive oxygen species metabolic process / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / negative regulation of cell growth / fatty acid biosynthetic process / NAD binding / FMN binding / nervous system development / 4 iron, 4 sulfur cluster binding / mitochondrial inner membrane / nuclear body / membrane / metal ion binding / cytosol
Similarity search - Function
NADH-ubiquinone oxidoreductase flavoprotein 3 / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / Zinc finger, CHCC-type / Zinc-finger domain / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / NADH:ubiquinone oxidoreductase subunit B14.5a (Complex I-B14.5a) / GRIM-19 / GRIM-19 protein / NDUFA6, LYR domain ...NADH-ubiquinone oxidoreductase flavoprotein 3 / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / Zinc finger, CHCC-type / Zinc-finger domain / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / NADH:ubiquinone oxidoreductase subunit B14.5a (Complex I-B14.5a) / GRIM-19 / GRIM-19 protein / NDUFA6, LYR domain / NADH dehydrogenase ubiquinone Fe-S protein 4-like superfamily / NADH dehydrogenase ubiquinone Fe-S protein 4 / NADH dehydrogenase ubiquinone Fe-S protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 2 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH ubiquinone oxidoreductase subunit NDUFA12 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / ETC complex I subunit conserved region / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 6 / NADH-quinone oxidoreductase, chain G, C-terminal / NADH-ubiquinone oxidoreductase subunit G, C-terminal / Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. / NADH-ubiquinone oxidoreductase, 20 Kd subunit / NADH-quinone oxidoreductase, chain I / NAD(P)H-quinone oxidoreductase subunit D/H / NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 49 Kd subunit signature. / NADH-quinone oxidoreductase, subunit D / Respiratory-chain NADH dehydrogenase, 49 Kd subunit / NADH:ubiquinone oxidoreductase, subunit G / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. / NADH dehydrogenase, subunit C / NADH ubiquinone oxidoreductase, F subunit / Complex 1 LYR protein domain / NADH:ubiquinone oxidoreductase, 30kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 30 Kd subunit signature. / Complex 1 protein (LYR family) / 2Fe-2S iron-sulfur cluster binding domain / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. / NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site / NADH:ubiquinone oxidoreductase, 30kDa subunit / NADH:ubiquinone oxidoreductase, 30kDa subunit superfamily / Respiratory-chain NADH dehydrogenase, 30 Kd subunit / Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. / NuoE domain / NADH-quinone oxidoreductase subunit E-like / Thioredoxin-like [2Fe-2S] ferredoxin / NADH-quinone oxidoreductase subunit E, N-terminal / NADH:ubiquinone oxidoreductase, 51kDa subunit, conserved site / Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. / NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain / NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding / NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain / NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain superfamily / NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily / Respiratory-chain NADH dehydrogenase 51 Kd subunit / NADH-ubiquinone oxidoreductase-F iron-sulfur binding region / His(Cys)3-ligated-type [4Fe-4S] domain profile. / NADH-ubiquinone oxidoreductase-F iron-sulfur binding region / Molybdopterin oxidoreductase, 4Fe-4S domain / Prokaryotic molybdopterin oxidoreductases 4Fe-4S domain profile. / NAD-dependent epimerase/dehydratase / NADH:ubiquinone oxidoreductase-like, 20kDa subunit / NADH ubiquinone oxidoreductase, 20 Kd subunit / NAD dependent epimerase/dehydratase family / Molybdopterin oxidoreductase / Molybdopterin oxidoreductase / [NiFe]-hydrogenase, large subunit / Ribosomal protein/NADH dehydrogenase domain / Mitochondrial ribosomal protein L51 / S25 / CI-B8 domain / Mitochondrial ribosomal protein L51 / S25 / CI-B8 domain / Acyl carrier protein (ACP) / 4Fe-4S dicluster domain / 2Fe-2S ferredoxin-type iron-sulfur binding domain profile. / 2Fe-2S ferredoxin-type iron-sulfur binding domain / 2Fe-2S ferredoxin-like superfamily / Phosphopantetheine attachment site / Phosphopantetheine attachment site. / 4Fe-4S ferredoxin, iron-sulphur binding, conserved site / 4Fe-4S ferredoxin-type iron-sulfur binding region signature. / 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. / 4Fe-4S ferredoxin-type, iron-sulphur binding domain / Phosphopantetheine attachment site / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain / Thioredoxin-like superfamily / NAD(P)-binding domain superfamily
Similarity search - Domain/homology
NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / Acyl carrier protein ...NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / Acyl carrier protein / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 / NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Similarity search - Component
Biological speciesSus scrofa (pig) / pig (pig) / Pig (pig)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.4 Å
AuthorsGu JK / Yang MJ
Funding support China, 2 items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2017YFA0504600 and 2016YFA0501100 China
National Natural Science Foundation of China (NSFC)31625008, 32030056, 21532004, 31570733, 31800620 China
CitationJournal: Nat Struct Mol Biol / Year: 2022
Title: The coupling mechanism of mammalian mitochondrial complex I.
Authors: Jinke Gu / Tianya Liu / Runyu Guo / Laixing Zhang / Maojun Yang /
Abstract: Mammalian respiratory complex I (CI) is a 45-subunit, redox-driven proton pump that generates an electrochemical gradient across the mitochondrial inner membrane to power ATP synthesis in ...Mammalian respiratory complex I (CI) is a 45-subunit, redox-driven proton pump that generates an electrochemical gradient across the mitochondrial inner membrane to power ATP synthesis in mitochondria. In the present study, we report cryo-electron microscopy structures of CI from Sus scrofa in six treatment conditions at a resolution of 2.4-3.5 Å, in which CI structures of each condition can be classified into two biochemical classes (active or deactive), with a notably higher proportion of active CI particles. These structures illuminate how hydrophobic ubiquinone-10 (Q10) with its long isoprenoid tail is bound and reduced in a narrow Q chamber comprising four different Q10-binding sites. Structural comparisons of active CI structures from our decylubiquinone-NADH and rotenone-NADH datasets reveal that Q10 reduction at site 1 is not coupled to proton pumping in the membrane arm, which might instead be coupled to Q10 oxidation at site 2. Our data overturn the widely accepted previous proposal about the coupling mechanism of CI.
History
DepositionAug 31, 2021-
Header (metadata) releaseApr 6, 2022-
Map releaseApr 6, 2022-
UpdateApr 6, 2022-
Current statusApr 6, 2022Processing site: PDBj / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_31883.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 0.5371 Å
Density
Contour LevelBy AUTHOR: 0.014
Minimum - Maximum-0.045928396 - 0.08689895
Average (Standard dev.)0.00011864873 (±0.0022168916)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 274.9952 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Sample components

+
Entire : Respiratory complex I

EntireName: Respiratory complex I
Components
  • Complex: Respiratory complex I
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
    • Protein or peptide: Acyl carrier protein, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
    • Protein or peptide: NADH dehydrogenase ubiquinone 1 alpha subcomplex subunit 9, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
    • Protein or peptide: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
  • Ligand: IRON/SULFUR CLUSTERIron–sulfur cluster
  • Ligand: FLAVIN MONONUCLEOTIDE
  • Ligand: 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE
  • Ligand: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine
  • Ligand: (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL
  • Ligand: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate
  • Ligand: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: MAGNESIUM ION
  • Ligand: CARDIOLIPIN
  • Ligand: ZINC ION
  • Ligand: water

+
Supramolecule #1: Respiratory complex I

SupramoleculeName: Respiratory complex I / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#18
Source (natural)Organism: Sus scrofa (pig)

+
Macromolecule #1: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 47.265875 KDa
SequenceString: KKTSFGSLKD EDRIFTNLYG RHDWRLKGAQ SRGDWYKTKE ILLKGPDWIL GEVKTSGLRG RGGAGFPTGL KWSFMNKPSD GRPKYLVVN ADEGEPGTCK DREIIRHDPH KLVEGCLVGG RAMGARAAYI YIRGEFYNEA SNLQVAIREA YEAGLIGKNA C GSGYDFDV ...String:
KKTSFGSLKD EDRIFTNLYG RHDWRLKGAQ SRGDWYKTKE ILLKGPDWIL GEVKTSGLRG RGGAGFPTGL KWSFMNKPSD GRPKYLVVN ADEGEPGTCK DREIIRHDPH KLVEGCLVGG RAMGARAAYI YIRGEFYNEA SNLQVAIREA YEAGLIGKNA C GSGYDFDV FVVRGAGAYI CGEETALIES IEGKQGKPRL KPPFPADVGV FGCPTTVANV ETVAVSPTIC RRGGAWFASF GR ERNSGTK LFNISGHVNH PCTVEEEMSV PLKELIEKHA GGVIGGWDNL LAVIPGGSST PLIPKSVCET VLMDFDALVQ AQT GLGTAA VIVMDRSTDI VKAIARLIEF YKHESCGQCT PCREGVDWMN KVMARFVKGD ARPAEIDSLW EISKQIEGHT ICAL GDGAA WPVQGLIRHF RPELEERMQQ FALQHQ

+
Macromolecule #2: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 20.207957 KDa
SequenceString:
TYKFVNMREP SMDMKSVTDR AAQTLLWTEL VRGLGMTLSY LFREPATINY PFEKGPLSPR FRGEHALRRY PSGEERCIAC KLCEAVCPA QAITIEAEPR ADGSRRTTRY DIDMTKCIYC GFCQEACPVD AIVEGPNFEF STETHEELLY NKEKLLNNGD K WEAEIAAN IQADYLYR

+
Macromolecule #3: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 17.874953 KDa
SequenceString:
SRGEYVVAKL DDLVNWARRS SLWPMTFGLA CCAVEMMHMA APRYDMDRFG VVFRASPRQS DVMIVAGTLT NKMAPALRKV YDQMPEPRY VVSMGSCANG GGYYHYSYSV VRGCDRIVPV DIYVPGCPPT AEALLYGILQ LQRKIKREKR LRIWYRR

+
Macromolecule #4: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 13.812977 KDa
SequenceString:
GTSVKPIFSR DMNEAKRRVR ELYRAWYREV PNTVHLFQLD ISVKQGRDKV REMFMKNAHV TDPRVVDLLV IKGKMELEET INVWKQRTH IMRFFHETEA PRPTDFLSKF YVGHDP

+
Macromolecule #5: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 9.84128 KDa
SequenceString:
LGLREIRIHL CQRSPGSQGV RDFIEKRYVE LKKANPDLPI LIRECSDVQP KLWARYAFGQ EKNVSLNNFS ADQVTRTLEN VLSGKA

+
Macromolecule #6: Acyl carrier protein, mitochondrial

MacromoleculeName: Acyl carrier protein, mitochondrial / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 10.133566 KDa
SequenceString:
SDAPPLTLEA IKDRVLYVLK LYDKIDPEKL SVNSHFMKDL GLDSLDQVEI IMAMEDEFGF EIPDIDAEKL MCPQEIVDYI ADKKDVYE

+
Macromolecule #7: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 12.949106 KDa
SequenceString:
LKKTTGLVGL AVCETPHERL KILYTKILDV LGQIPKNAAY RKYTEQITNE KLGMVKAEPD VKKLEEQLQG GQIEEVILQA ENELSLARK MLRWKPWEPL VEEPPANQWK WPI

+
Macromolecule #8: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 12.517394 KDa
SequenceString:
ASATRVIQLL RNWASGRDLQ AKLQLRYQEI SKRTQPPPKL PVGPSHKLSN NYYCTRDGRR EAMPPSIVMS SQKVLASGKP AESSAVAET EKKAVTPAPP IKRWELSKDQ PYL

+
Macromolecule #9: NADH dehydrogenase ubiquinone 1 alpha subcomplex subunit 9, mitoc...

MacromoleculeName: NADH dehydrogenase ubiquinone 1 alpha subcomplex subunit 9, mitochondrial
type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Pig (pig)
Molecular weightTheoretical: 38.840895 KDa
SequenceString: LHHALIPHGK GGRSSVSGIV ATVFGATGFL GRYVVNHLGR MGSQVIVPYR CEPYDTMHLR PMGDLGQIIF MEWNGKDKDS IRKVVEHSN VVINLVGREW ETKNFDFEDV FVKIPHAIAQ VSKEAGVEKL IHISHLNADI KSPSRYLRSK AVGEKEVRAA F PEATIIKP ...String:
LHHALIPHGK GGRSSVSGIV ATVFGATGFL GRYVVNHLGR MGSQVIVPYR CEPYDTMHLR PMGDLGQIIF MEWNGKDKDS IRKVVEHSN VVINLVGREW ETKNFDFEDV FVKIPHAIAQ VSKEAGVEKL IHISHLNADI KSPSRYLRSK AVGEKEVRAA F PEATIIKP SDIFGREDRF LNYFASMRWF GGVPLISLGK ETVKQPVYIV DVSKGIINAI KDPDAKGKTF AFVGPNRYLL FD LVQYIFA VAYRPFLPYP LPHFAYRWVG RLFEVSPFEP WTTRDKVERV HMSDMTLPHL PGLEDLGIQA TPLELKAIEV LRR HRTYRW LTSEMEDVKP AKTVN

+
Macromolecule #10: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial
type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 5.046509 KDa
SequenceString:
DNSTYRNLQH HEYSTYTFLD LNVELSKFRM PQPSSGRQSP RH

+
Macromolecule #11: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 14.442389 KDa
SequenceString:
QLIAVDEKLD ITTLTGVPEE HIKTRKVRIF VPARNNMQSG VNNTKKWKME FDTRERWENP LMGWSSTADP LSNLVLTFST KEDAVAFAE KNGWSFDVEE RKVPKPKSKS YGANFSWNKR TRVSTK

+
Macromolecule #12: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

MacromoleculeName: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 75.770773 KDa
SequenceString: SNLIEVFVDG QSVMVEPGTT VLQACEKVGM QIPRFCYHER LSVAGNCRMC LVEIEKAPKV VAACAMPVMK GWNILTNSEK SKKAREGVM EFLLANHPLD CPICDQGGEC DLQDQSMMFG SDRSRFLEGK RAVEDKNIGP LVKTIMTRCI QCTRCIRFAS E IAGVDDLG ...String:
SNLIEVFVDG QSVMVEPGTT VLQACEKVGM QIPRFCYHER LSVAGNCRMC LVEIEKAPKV VAACAMPVMK GWNILTNSEK SKKAREGVM EFLLANHPLD CPICDQGGEC DLQDQSMMFG SDRSRFLEGK RAVEDKNIGP LVKTIMTRCI QCTRCIRFAS E IAGVDDLG TTGRGNDMQV GTYIEKMFMS ELSGNIIDIC PVGALTSKPY AFTARPWETR KTESIDVMDA VGSNIVVSTR TG EVMRILP RMHEDINEEW ISDKTRFAYD GLKRQRLTQP MIRNEKGLLT YTTWEDALSR VAGMLQSFQG NDVAAIAGGL VDA EALVAL KDLLNRVDSD SLCTEEVFPT AGAGTDLRSN YLLNTTIAGV EEADVILLVG TNPRFEAPLF NARIRKSWLH NDLK VALIG SPVDLTYRYD HLGDSPKILQ DIASGNHPFS QILKEAKKPM VVLGSSALQR SDGTAILAAV SNIAQNIRLS SGVTG DWKV MNILHRIASQ VAALDLGYKP GVEAIRKNPP KVLFLLGADG GCITRQDLPK DCFIIYQGHH GDVGAPMADV ILPGAA YTE KSATYVNTEG RAQQTKVAVT PPGLAREDWK IIRALSEIAG MTLPYDTLDQ VRSRLEEVSP NLVRYDDVEG ANYFQQA NE LSKLVNQQLL ADPLVPPQLT IKDFYMTDSI SRASQTMAKC VKAVTEGI

+
Macromolecule #13: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 17.031244 KDa
SequenceString:
ELVQVLRRGL QQVSGHGGLR GYLRVLFRAN DVRVGTLVGE DKYGNKYYED NKQFFGRHRW VIYTTEMNGR DTFWDVDGSM VPPEWHRWL HCMTDDPPTT KPPTARKYIW TNHKFNVSGT PQQYVPYSTT RKKIQEWVPP STPYK

+
Macromolecule #14: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 23.826336 KDa
SequenceString: GAGGALFVHR DTPENNPDTP FDFTPENYKR IEAIVKNYPE GHKAAAVLPV LDLAQRQNGW LPISAMNKVA EILQVPPMRV YEVATFYTM YNRKPVGKYH IQVCTTTPCM LRNSDSILEA IQKKLGIKVG ETTPDKLFTL IEVECLGACV NAPMVQINDN Y YEDLTPKD ...String:
GAGGALFVHR DTPENNPDTP FDFTPENYKR IEAIVKNYPE GHKAAAVLPV LDLAQRQNGW LPISAMNKVA EILQVPPMRV YEVATFYTM YNRKPVGKYH IQVCTTTPCM LRNSDSILEA IQKKLGIKVG ETTPDKLFTL IEVECLGACV NAPMVQINDN Y YEDLTPKD IEEIIDELKA GKIPKPGPRS GRFSCEPAGG LTSLTEPPKG PGFGVQAGL

+
Macromolecule #15: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial
type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 24.52173 KDa
SequenceString: TRPTIRPRND VVHKQLSAFG QYVAEILPKY VQQVQVSCFN ELEIFIHPDG VIPVLTFLRD HTNAQFKSLA DLTAVDVPTR QNRFEIVYN LLSLRFNSRI RVKTYTDELT PIESSVTVYK AANWYEREIW DMFGVFFANH PDLRRILTDY GFEGHPFRKD F PLSGYVEL ...String:
TRPTIRPRND VVHKQLSAFG QYVAEILPKY VQQVQVSCFN ELEIFIHPDG VIPVLTFLRD HTNAQFKSLA DLTAVDVPTR QNRFEIVYN LLSLRFNSRI RVKTYTDELT PIESSVTVYK AANWYEREIW DMFGVFFANH PDLRRILTDY GFEGHPFRKD F PLSGYVEL RYDDEVKRVV AEPVELAQEF RKFDLNSPWE AFPAYRQPPE

+
Macromolecule #16: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 44.040613 KDa
SequenceString: NLTLNFGPQH PAAHGVLRLV MELSGEMVRK CDPHIGLLH(2MR) GTEKLIEYKT YLQALPYFDR LDYVSMMCNE QAYSLA VEK LLNIQPPPRA QWIRVLFGEI TRLLNHIMAV TTHALDIGAM TPFFWMFEER EKMFEFYERV SGARMHAAYI RPGGVHQ DL PLGLLDDIYE ...String:
NLTLNFGPQH PAAHGVLRLV MELSGEMVRK CDPHIGLLH(2MR) GTEKLIEYKT YLQALPYFDR LDYVSMMCNE QAYSLA VEK LLNIQPPPRA QWIRVLFGEI TRLLNHIMAV TTHALDIGAM TPFFWMFEER EKMFEFYERV SGARMHAAYI RPGGVHQ DL PLGLLDDIYE FSKNFSFRID ELEEMLTNNR IWRNRTVDIG VVTAEDALNY GFSGVMLRGS GIQWDLRKTQ PYDVYDQV E FDVPIGSRGD CYDRYLCRVE EMRQSLRIIS QCLNKMPPGE IKVDDAKVSP PKRAEMKTSM ESLIHHFKLY TEGYQVPPG ATYTAIEAPK GEFGVYLVSD GSSRPYRCKI KAPGFAHLAG LDKMSKGHML ADVVAIIGTQ DIVFGEVDR

+
Macromolecule #17: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 10.567635 KDa
SequenceString:
GVRTSPTGEK VTHTGQAYDD GDYRRVRFSD RQKEVNENFA IDLIAEQPVS EVGSRVISCD GGGGALGHPR VYINLDKETK TGTCGYCGL QFRQPHH

+
Macromolecule #18: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 3.204705 KDa
SequenceString:
ASKVKQDMPP PGGYGPIDYK RNLPRRGLS

+
Macromolecule #19: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 19 / Number of copies: 6 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

ChemComp-FS1:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

+
Macromolecule #20: FLAVIN MONONUCLEOTIDE

MacromoleculeName: FLAVIN MONONUCLEOTIDE / type: ligand / ID: 20 / Number of copies: 1 / Formula: FMN
Molecular weightTheoretical: 456.344 Da
Chemical component information

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE / Flavin mononucleotide

+
Macromolecule #21: 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE

MacromoleculeName: 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE / type: ligand / ID: 21 / Number of copies: 1 / Formula: NAI
Molecular weightTheoretical: 665.441 Da
Chemical component information

ChemComp-NAI:
1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE / Nicotinamide adenine dinucleotide

+
Macromolecule #22: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine

MacromoleculeName: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / type: ligand / ID: 22 / Number of copies: 1 / Formula: PEE
Molecular weightTheoretical: 744.034 Da
Chemical component information

ChemComp-PEE:
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipid*YM / Discrete optimized protein energy

+
Macromolecule #23: (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,...

MacromoleculeName: (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL
type: ligand / ID: 23 / Number of copies: 1 / Formula: PLX
Molecular weightTheoretical: 767.132 Da
Chemical component information

ChemComp-PLX:
(9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL / phospholipid*YM

+
Macromolecule #24: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-b...

MacromoleculeName: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate
type: ligand / ID: 24 / Number of copies: 1 / Formula: 8Q1
Molecular weightTheoretical: 540.651 Da
Chemical component information

ChemComp-8Q1:
S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate

+
Macromolecule #25: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

MacromoleculeName: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
type: ligand / ID: 25 / Number of copies: 1 / Formula: NDP
Molecular weightTheoretical: 745.421 Da
Chemical component information

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / Nicotinamide adenine dinucleotide phosphate

+
Macromolecule #26: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 26 / Number of copies: 2 / Formula: FES
Molecular weightTheoretical: 175.82 Da
Chemical component information

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster

+
Macromolecule #27: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 27 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

+
Macromolecule #28: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 28 / Number of copies: 1 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

+
Macromolecule #29: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 29 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

+
Macromolecule #30: water

MacromoleculeName: water / type: ligand / ID: 30 / Number of copies: 713 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER / Water

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.3 µm
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Initial angle assignmentType: RANDOM ASSIGNMENT
Final angle assignmentType: RANDOM ASSIGNMENT
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 387112

+
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