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- EMDB-18616: E2/E3BP core of the human pyruvate dehydrogenase complex (map 1; ... -
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Open data
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Basic information
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Title | E2/E3BP core of the human pyruvate dehydrogenase complex (map 1; 3.4 A) | |||||||||
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![]() | pyruvate dehydrogenase complex / PDHc / E2 / E3BP / cryo-EM / TRANSFERASE | |||||||||
Function / homology | ![]() dihydrolipoyllysine-residue acetyltransferase / dihydrolipoyllysine-residue acetyltransferase activity / acetyl-CoA biosynthetic process from pyruvate / : / pyruvate dehydrogenase complex / Pyruvate metabolism / Glyoxylate metabolism and glycine degradation / Regulation of pyruvate dehydrogenase (PDH) complex / Signaling by Retinoic Acid / acyltransferase activity ...dihydrolipoyllysine-residue acetyltransferase / dihydrolipoyllysine-residue acetyltransferase activity / acetyl-CoA biosynthetic process from pyruvate / : / pyruvate dehydrogenase complex / Pyruvate metabolism / Glyoxylate metabolism and glycine degradation / Regulation of pyruvate dehydrogenase (PDH) complex / Signaling by Retinoic Acid / acyltransferase activity / tricarboxylic acid cycle / glucose metabolic process / mitochondrial matrix / intracellular membrane-bounded organelle / mitochondrion / identical protein binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
![]() | Zdanowicz R / Afanasyev P / Boehringer D / Glockshuber R | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Stoichiometry and architecture of the human pyruvate dehydrogenase complex Authors: Zdanowicz R / Afanasyev P / Pruska A / Harrison JA / Boehringer D / Leitner A / Zenobi R / Glockshuber R | |||||||||
History |
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Structure visualization
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Downloads & links
-EMDB archive
Header (meta data) | ![]() | |||
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Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 760 KB | Display | ![]() |
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Full document | ![]() | 759.6 KB | Display | |
Data in XML | ![]() | 20.2 KB | Display | |
Data in CIF | ![]() | 26.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 17691 ![]() 17694 ![]() 18617 ![]() 8piuC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | Released | ||||||||||||||||||||
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Voxel size | X=Y=Z: 1.0929 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : E2/E3BP core of the human pyruvate dehydrogenase complex
Entire | Name: E2/E3BP core of the human pyruvate dehydrogenase complex |
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Components |
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-Supramolecule #1: E2/E3BP core of the human pyruvate dehydrogenase complex
Supramolecule | Name: E2/E3BP core of the human pyruvate dehydrogenase complex type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 3.4 MDa |
-Macromolecule #1: Dihydrolipoyllysine-residue acetyltransferase component of pyruva...
Macromolecule | Name: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex type: protein_or_peptide / ID: 1 / Enantiomer: LEVO / EC number: dihydrolipoyllysine-residue acetyltransferase |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MHHHHHHENL YFQSLPPHQK VPLPSLSPTM QAGTIARWEK KEGDKINEGD LIAEVETDKA TVGFESLEEC YMAKILVAEG TRDVPIGAII CITVGKPEDI EAFKNYTLDS SAAPTPQAAP APTPAATASP PTPSAQAPGS SYPPHMQVLL PALSPTMTMG TVQRWEKKVG ...String: MHHHHHHENL YFQSLPPHQK VPLPSLSPTM QAGTIARWEK KEGDKINEGD LIAEVETDKA TVGFESLEEC YMAKILVAEG TRDVPIGAII CITVGKPEDI EAFKNYTLDS SAAPTPQAAP APTPAATASP PTPSAQAPGS SYPPHMQVLL PALSPTMTMG TVQRWEKKVG EKLSEGDLLA EIETDKATIG FEVQEEGYLA KILVPEGTRD VPLGTPLCII VEKEADISAF ADYRPTEVTD LKPQVPPPTP PPVAAVPPTP QPLAPTPSAP CPATPAGPKG RVFVSPLAKK LAVEKGIDLT QVKGTGPDGR ITKKDIDSFV PSKVAPAPAA VVPPTGPGMA PVPTGVFTDI PISNIRRVIA QRLMQSKQTI PHYYLSIDVN MGEVLLVRKE LNKILEGRSK ISVNDFIIKA SALACLKVPE ANSSWMDTVI RQNHVVDVSV AVSTPAGLIT PIVFNAHIKG VETIANDVVS LATKAREGKL QPHEFQGGTF TISNLGMFGI KNFSAIINPP QACILAIGAS EDKLVPADNE KGFDVASMMS VTLSCDHRVV DGAVGAQWLA EFRKYLEKPI TMLL UniProtKB: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial |
-Macromolecule #2: Pyruvate dehydrogenase protein X component
Macromolecule | Name: Pyruvate dehydrogenase protein X component / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MGDPIKILMP SLSPTMEEGN IVKWLKKEGE AVSAGDALCE IETDKAVVTL DASDDGILAK IVVEEGSKNI RLGSLIGLIV EEGEDWKHVE IPKDVGPPPP VSKPSEPRPS PEPQISIPVK KEHIPGTLRF RLSPAARNIL EKHSLDASQG TATGPRGIFT KEDALKLVQL ...String: MGDPIKILMP SLSPTMEEGN IVKWLKKEGE AVSAGDALCE IETDKAVVTL DASDDGILAK IVVEEGSKNI RLGSLIGLIV EEGEDWKHVE IPKDVGPPPP VSKPSEPRPS PEPQISIPVK KEHIPGTLRF RLSPAARNIL EKHSLDASQG TATGPRGIFT KEDALKLVQL KQTGKITESR PTPAPTATPT APSPLQATAG PSYPRPVIPP VSTPGQPNAV GTFTEIPASN IRRVIAKRLT ESKSTVPHAY ATADCDLGAV LKVRQDLVKD DIKVSVNDFI IKAAAVTLKQ MPDVNVSWDG EGPKQLPFID ISVAVATDKG LLTPIIKDAA AKGIQEIADS VKALSKKARD GKLLPEEYQG GSFSISNLGM FGIDEFTAVI NPPQACILAV GRFRPVLKLT EDEEGNAKLQ QRQLITVTMS SDSRVVDDEL ATRFLKSFKA NLENPIRLA UniProtKB: Pyruvate dehydrogenase protein X component, mitochondrial |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Grid | Model: Quantifoil R2/2 / Material: COPPER / Support film - Material: CARBON / Support film - topology: HOLEY |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Detector mode: COUNTING / Average electron dose: 80.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 1.6 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: OTHER / Details: RELION 3D initial model |
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Final reconstruction | Applied symmetry - Point group: T (tetrahedral) / Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 3.2) / Number images used: 513329 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1) |
Final angle assignment | Type: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1) |