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- PDB-5xtc: Cryo-EM structure of human respiratory complex I transmembrane arm -

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Entry
Database: PDB / ID: 5xtc
TitleCryo-EM structure of human respiratory complex I transmembrane arm
Components
  • (NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit ...) x 6
  • (NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit ...) x 11
  • (NADH dehydrogenase [ubiquinone] 1 subunit ...) x 2
  • (NADH dehydrogenase [ubiquinone] iron-sulfur protein ...) x 2
  • (NADH-ubiquinone oxidoreductase chain ...) x 7
  • Acyl carrier protein, mitochondrial
KeywordsELECTRON TRANSPORT / Homo sapiens / Oxidoreductase / Respiratory / Complex
Function / homologyNADH dehydrogenase subunit 2, C-terminal / NADH:ubiquinone oxidoreductase, ESSS subunit / NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, metazoa / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 8 / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex subunit 1 / NADH:ubiquinone oxidoreductase, subunit 1, conserved site / NADH:ubiquinone oxidoreductase, NDUFB5/SGDH subunit / NADH dehydrogenase 1, beta subcomplex, subunit 6 ...NADH dehydrogenase subunit 2, C-terminal / NADH:ubiquinone oxidoreductase, ESSS subunit / NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, metazoa / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 8 / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex subunit 1 / NADH:ubiquinone oxidoreductase, subunit 1, conserved site / NADH:ubiquinone oxidoreductase, NDUFB5/SGDH subunit / NADH dehydrogenase 1, beta subcomplex, subunit 6 / NADH:ubiquinone oxidoreductase, iron-sulphur subunit 5 / NADH:ubiquinone oxidoreductase, MNLL subunit / NADH-ubiquinone oxidoreductase, subunit 10 / NAD(P)H-quinone oxidoreductase subunit D/H / NADH-ubiquinone oxidoreductase 1 subunit C1 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2 / P-loop containing nucleoside triphosphate hydrolase / [NiFe]-hydrogenase, large subunit / Deoxynucleoside kinase domain / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 / NADH dehydrogenase subunit 5, C-terminal / NADH-plastoquinone oxidoreductase, chain 5 / NADH:ubiquinone/plastoquinone oxidoreductase, chain 3 / NADH:ubiquinone oxidoreductase, chain 2 / Acyl carrier protein (ACP) / NADH:quinone oxidoreductase/Mrp antiporter, membrane subunit / NADH:ubiquinone oxidoreductase, subunit 1/F420H2 oxidoreductase subunit H / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminal / NADH:ubiquinone/plastoquinone oxidoreductase, chain 6 / NADH-quinone oxidoreductase, subunit D / NADH-ubiquinone oxidoreductase chain 4L/K / NADH:ubiquinone oxidoreductase chain 4, N-terminal / CHCH / Phosphopantetheine attachment site / Complex 1 LYR protein / NADH:ubiquinone oxidoreductase, B18 subunit / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8 / Phosphopantetheine binding ACP domain / GRIM-19 / NADH:ubiquinone oxidoreductase, subunit b14.5b / NADH:ubiquinone oxidoreductase, subunit NDUFB4 / NADH-quinone oxidoreductase, chain M/4 / ACP-like superfamily / NADH-quinone oxidoreductase, subunit D superfamily / NADH:ubiquinone oxidoreductase, subunit 3 superfamily / Respiratory chain NADH dehydrogenase 49 Kd subunit signature. / ESSS subunit of NADH:ubiquinone oxidoreductase (complex I) / NADH:ubiquinone oxidoreductase, NDUFS5-15kDa / NADH-ubiquinone oxidoreductase subunit 10 / NADH dehydrogenase 1 beta subcomplex subunit 2 / NADH dehydrogenase 1 alpha subcomplex subunit 3 / NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial / NADH-ubiquinone oxidoreductase MWFE subunit / Phosphopantetheine attachment site. / Respiratory-chain NADH dehydrogenase subunit 1 signature 1. / NADH:ubiquinone oxidoreductase, NDUFB5/SGDH subunit / Respiratory-chain NADH dehydrogenase subunit 1 signature 2. / Carrier protein (CP) domain profile. / Coiled coil-helix-coiled coil-helix (CHCH) domain profile. / Mitochondrial protein import / Glyoxylate metabolism and glycine degradation / Respiratory electron transport / Neutrophil degranulation / Complex I biogenesis / Mitochondrial Fatty Acid Beta-Oxidation / NADH:ubiquinone oxidoreductase, NDUFB6/B17 subunit / NADH-ubiquinone oxidoreductase B12 subunit family / NADH dehydrogenase / NADH-ubiquinone oxidoreductase B18 subunit (NDUFB7) / Respiratory-chain NADH dehydrogenase, 49 Kd subunit / Proton-conducting membrane transporter / NADH-ubiquinone/plastoquinone oxidoreductase chain 6 / NADH-ubiquinone/plastoquinone oxidoreductase, chain 3 / Phosphopantetheine attachment site / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus / NADH-ubiquinone oxidoreductase chain 4, amino terminus / Deoxynucleoside kinase / Complex 1 protein (LYR family) / NADH:ubiquinone oxidoreductase / MNLL subunit / NADH-ubiquinone oxidoreductase ASHI subunit (CI-ASHI or NDUFB8) / GRIM-19 protein / NADH-ubiquinone oxidoreductase subunit b14.5b (NDUFC2) / NADH dehydrogenase subunit 2 C-terminus / NADH dehydrogenase subunit 5 C-terminus / CHCH domain / NADH-ubiquinone oxidoreductase B15 subunit (NDUFB4) / response to light intensity / positive regulation of peptidase activity / protein import into mitochondrial inner membrane / NADH dehydrogenase (ubiquinone) / NADH dehydrogenase / mitochondrial respiratory chain complex I / NADH dehydrogenase activity / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / protein lipoylation / cellular respiration
Function and homology information
Specimen sourceHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / 3.7 Å resolution
AuthorsGu, J. / Wu, M. / Yang, M.
CitationJournal: Cell / Year: 2017
Title: Architecture of Human Mitochondrial Respiratory Megacomplex IIIIIV.
Authors: Runyu Guo / Shuai Zong / Meng Wu / Jinke Gu / Maojun Yang
Abstract: The respiratory megacomplex represents the highest-order assembly of respiratory chain complexes, and it allows mitochondria to respond to energy-requiring conditions. To understand its architecture, ...The respiratory megacomplex represents the highest-order assembly of respiratory chain complexes, and it allows mitochondria to respond to energy-requiring conditions. To understand its architecture, we examined the human respiratory chain megacomplex-IIIIIV (MCIIIIIV) with 140 subunits and a subset of associated cofactors using cryo-electron microscopy. The MCIIIIIV forms a circular structure with the dimeric CIII located in the center, where it is surrounded by two copies each of CI and CIV. Two cytochrome c (Cyt.c) molecules are positioned to accept electrons on the surface of the c state CIII dimer. Analyses indicate that CII could insert into the gaps between CI and CIV to form a closed ring, which we termed the electron transport chain supercomplex. The structure not only reveals the precise assignment of individual subunits of human CI and CIII, but also enables future in-depth analysis of the electron transport chain as a whole.
Validation Report
SummaryFull reportAbout validation report
DateDeposition: Jun 19, 2017 / Release: Aug 30, 2017
RevisionDateData content typeGroupCategoryItemProviderType
1.0Aug 30, 2017Structure modelrepositoryInitial release
1.1Sep 6, 2017Structure modelDatabase referencescitation_citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.title / _citation.year
1.2Dec 6, 2017Structure modelData processing / Database referencescitation / em_software_citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _em_software.name

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Assembly

Deposited unit
Q: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
S: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
U: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3
V: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
W: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
X: Acyl carrier protein, mitochondrial
Y: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial
Z: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3
a: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial
b: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6
c: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial
d: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10
e: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial
f: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial
g: NADH dehydrogenase [ubiquinone] 1 subunit C2
h: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5
i: NADH-ubiquinone oxidoreductase chain 2
j: NADH-ubiquinone oxidoreductase chain 3
k: NADH-ubiquinone oxidoreductase chain 4L
l: NADH-ubiquinone oxidoreductase chain 5
m: NADH-ubiquinone oxidoreductase chain 6
n: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1
o: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
p: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
r: NADH-ubiquinone oxidoreductase chain 4
s: NADH-ubiquinone oxidoreductase chain 1
u: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
v: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
w: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)561,09648
Polyers543,33529
Non-polymers17,76119
Water0
1


TypeNameSymmetry operationNumber
identity operation1_5551
Buried area (Å2)182270
ΔGint (kcal/M)-1332
Surface area (Å2)178170

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Components

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NADH dehydrogenase [ubiquinone] iron-sulfur protein ... , 2 types, 2 molecules Qh

#1: Protein/peptide NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial / Complex I-49kD / CI-49kD / NADH-ubiquinone oxidoreductase 49 kDa subunit


Mass: 5380.995 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 34-79 / Source: (natural) Homo sapiens (human)
References: UniProt: O75306, NADH dehydrogenase (ubiquinone), NADH dehydrogenase
#16: Protein/peptide NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 / Complex I-15 kDa / CI-15 kDa / NADH-ubiquinone oxidoreductase 15 kDa subunit


Mass: 12314.254 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human) / References: UniProt: O43920

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NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit ... , 6 types, 6 molecules SUVWuw

#2: Protein/peptide NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 / Complex I-MWFE / CI-MWFE / NADH-ubiquinone oxidoreductase MWFE subunit


Mass: 8084.391 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human) / References: UniProt: O15239
#3: Protein/peptide NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3 / Complex I-B9 / CI-B9 / NADH-ubiquinone oxidoreductase B9 subunit


Mass: 9156.602 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human) / References: UniProt: O95167
#4: Protein/peptide NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 / Complex I-B14.7 / CI-B14.7 / NADH-ubiquinone oxidoreductase subunit B14.7


Mass: 14736.853 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human) / References: UniProt: Q86Y39
#5: Protein/peptide NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 / Cell death regulatory protein GRIM-19 / Complex I-B16.6 / CI-B16.6 / Gene associated with retinoic and interferon-induced mortality 19 protein / Gene associated with retinoic and IFN-induced mortality 19 protein / NADH-ubiquinone oxidoreductase B16.6 subunit


Mass: 13589.633 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 29-144 / Source: (natural) Homo sapiens (human) / References: UniProt: Q9P0J0
#27: Protein/peptide NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 / Complex I-19kD / CI-19kD / Complex I-PGIV / CI-PGIV / NADH-ubiquinone oxidoreductase 19 kDa subunit


Mass: 19853.736 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human) / References: UniProt: P51970
#29: Protein/peptide NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial / Complex I-42kD / CI-42kD / NADH-ubiquinone oxidoreductase 42 kDa subunit


Mass: 37200.270 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human) / References: UniProt: O95299

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Protein/peptide , 1 types, 1 molecules X

#6: Protein/peptide Acyl carrier protein, mitochondrial / ACP / CI-SDAP / NADH-ubiquinone oxidoreductase 9.6 kDa subunit


Mass: 9845.247 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human) / References: UniProt: O14561

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NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit ... , 11 types, 11 molecules YZabcdenopv

#7: Protein/peptide NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial / Complex I-AGGG / CI-AGGG / NADH-ubiquinone oxidoreductase AGGG subunit


Mass: 7468.270 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 39-97 / Source: (natural) Homo sapiens (human) / References: UniProt: O95178
#8: Protein/peptide NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 / Complex I-B12 / CI-B12 / NADH-ubiquinone oxidoreductase B12 subunit


Mass: 9261.605 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 10-89 / Source: (natural) Homo sapiens (human) / References: UniProt: O43676
#9: Protein/peptide NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial / Complex I-SGDH / CI-SGDH / NADH-ubiquinone oxidoreductase SGDH subunit


Mass: 16573.160 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human) / References: UniProt: O43674
#10: Protein/peptide NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6 / Complex I-B17 / CI-B17 / NADH-ubiquinone oxidoreductase B17 subunit


Mass: 15517.228 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human) / References: UniProt: O95139
#11: Protein/peptide NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial / Complex I-ASHI / CI-ASHI / NADH-ubiquinone oxidoreductase ASHI subunit


Mass: 18267.562 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human) / References: UniProt: O95169
#12: Protein/peptide NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 / Complex I-PDSW / CI-PDSW / NADH-ubiquinone oxidoreductase PDSW subunit


Mass: 20721.650 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human) / References: UniProt: O96000
#13: Protein/peptide NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial / Complex I-ESSS / CI-ESSS / NADH-ubiquinone oxidoreductase ESSS subunit / Neuronal protein 17.3 / p17.3


Mass: 11494.942 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 54-150 / Source: (natural) Homo sapiens (human) / References: UniProt: Q9NX14
#22: Protein/peptide NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1 / Complex I-MNLL / CI-MNLL / NADH-ubiquinone oxidoreductase MNLL subunit


Mass: 6741.883 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human) / References: UniProt: O75438
#23: Protein/peptide NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4 / Complex I-B15 / CI-B15 / NADH-ubiquinone oxidoreductase B15 subunit


Mass: 15100.399 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human) / References: UniProt: O95168
#24: Protein/peptide NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / Complex I-B22 / CI-B22 / LYR motif-containing protein 3 / NADH-ubiquinone oxidoreductase B22 subunit


Mass: 21189.141 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y6M9
#28: Protein/peptide NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 / Cell adhesion protein SQM1 / Complex I-B18 / CI-B18 / NADH-ubiquinone oxidoreductase B18 subunit


Mass: 14997.401 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human) / References: UniProt: P17568

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NADH dehydrogenase [ubiquinone] 1 subunit ... , 2 types, 2 molecules fg

#14: Protein/peptide NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial / Complex I-KFYI / CI-KFYI / NADH-ubiquinone oxidoreductase KFYI subunit


Mass: 5704.602 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human) / References: UniProt: O43677
#15: Protein/peptide NADH dehydrogenase [ubiquinone] 1 subunit C2 / Complex I-B14.5b / CI-B14.5b / Human lung cancer oncogene 1 protein / HLC-1 / NADH-ubiquinone oxidoreductase subunit B14.5b


Mass: 14209.521 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human) / References: UniProt: O95298

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NADH-ubiquinone oxidoreductase chain ... , 7 types, 7 molecules ijklmrs

#17: Protein/peptide NADH-ubiquinone oxidoreductase chain 2


Mass: 39007.656 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human)
References: UniProt: Q4GRX1, UniProt: P03891*PLUS, NADH dehydrogenase (ubiquinone)
#18: Protein/peptide NADH-ubiquinone oxidoreductase chain 3


Mass: 13147.871 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human)
References: UniProt: B9EE38, UniProt: P03897*PLUS, NADH dehydrogenase (ubiquinone)
#19: Protein/peptide NADH-ubiquinone oxidoreductase chain 4L


Mass: 10702.086 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human)
References: UniProt: V9JN72, UniProt: P03901*PLUS, NADH dehydrogenase (ubiquinone)
#20: Protein/peptide NADH-ubiquinone oxidoreductase chain 5


Mass: 67096.023 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human)
References: UniProt: X5BVZ3, UniProt: P03915*PLUS, NADH dehydrogenase (ubiquinone)
#21: Protein/peptide NADH-ubiquinone oxidoreductase chain 6


Mass: 18660.979 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human)
References: UniProt: Q8HAX7, UniProt: P03923*PLUS, NADH dehydrogenase (ubiquinone)
#25: Protein/peptide NADH-ubiquinone oxidoreductase chain 4


Mass: 51689.688 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human)
References: UniProt: B2XJG5, UniProt: P03905*PLUS, NADH dehydrogenase (ubiquinone)
#26: Protein/peptide NADH-ubiquinone oxidoreductase chain 1


Mass: 35621.215 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human)
References: UniProt: H9PGF0, UniProt: P03886*PLUS, NADH dehydrogenase (ubiquinone)

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Non-polymers , 4 types, 19 molecules

#30: Chemical
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


Mass: 767.132 Da / Num. of mol.: 9 / Formula: C42H89NO8P
#31: 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.: 5 / Formula: C81H156O17P2 / Cardiolipin / Comment: phospholipid *YM
#32: Chemical
ChemComp-PEE / 1,2-Dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE


Mass: 749.073 Da / Num. of mol.: 4 / Formula: C41H83NO8P / Discrete optimized protein energy / Comment: DOPE (phospholipid) *YM
#33: Chemical ChemComp-8Q1 / S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate / S-dodecanoyl-4'-phosphopantetheine


Mass: 540.651 Da / Num. of mol.: 1 / Formula: C23H45N2O8PS

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Experimental details

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Experiment

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

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Sample preparation

ComponentName: Human respiratory complex I transmembrane arm / Type: COMPLEX
Entity ID: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29
Source: NATURAL
Molecular weightExperimental value: NO
Source (natural)Organism: Homo sapiens (human)
Buffer solutionpH: 7.4
SpecimenConc.: 0.2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyMicroscope model: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER
Electron lensMode: BRIGHT FIELDBright-field microscopy
Image recordingElectron dose: 1.25 e/Å2 / Film or detector model: FEI FALCON II (4k x 4k)

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Processing

EM software
IDNameVersionCategory
1EMAN2.1particle selection
2AutoEMation2.0image acquisition
4CTFFIND3.0CTF correction
7Coot0.8.2model fitting
9RELION1.4initial Euler assignment
10RELION1.4final Euler assignment
11RELION1.4classification
12RELION1.43D reconstruction
13PHENIX1.11.1model refinement
CTF correctionType: NONE
SymmetryPoint symmetry: C1
3D reconstructionResolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 167761 / Symmetry type: POINT

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