+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-37969 | |||||||||
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Title | Structure of mitochondrial soluble protein | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Structure of mitochondrial enzyme complex / TRANSFERASE | |||||||||
Function / homology | Function and homology information dihydrolipoyllysine-residue acetyltransferase / dihydrolipoyllysine-residue acetyltransferase activity / acetyl-CoA biosynthetic process from pyruvate / pyruvate dehydrogenase complex / mitochondrial matrix Similarity search - Function | |||||||||
Biological species | Sus scrofa (pig) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.66 Å | |||||||||
Authors | Zhang SS / Chen MF | |||||||||
Funding support | China, 1 items
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Citation | Journal: Protein Cell / Year: 2024 Title: Molecular architecture of mammalian pyruvate dehydrogenase complex. Authors: Maofei Chen / Yutong Song / Sensen Zhang / Yitang Zhang / Xudong Chen / Minghui Zhang / Meng Han / Xin Gao / Sai Li / Maojun Yang / | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_37969.map.gz | 19.7 MB | EMDB map data format | |
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Header (meta data) | emd-37969-v30.xml emd-37969.xml | 13.2 KB 13.2 KB | Display Display | EMDB header |
Images | emd_37969.png | 141.5 KB | ||
Filedesc metadata | emd-37969.cif.gz | 5.1 KB | ||
Others | emd_37969_half_map_1.map.gz emd_37969_half_map_2.map.gz | 138.8 MB 138.8 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-37969 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-37969 | HTTPS FTP |
-Validation report
Summary document | emd_37969_validation.pdf.gz | 593 KB | Display | EMDB validaton report |
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Full document | emd_37969_full_validation.pdf.gz | 592.6 KB | Display | |
Data in XML | emd_37969_validation.xml.gz | 15.1 KB | Display | |
Data in CIF | emd_37969_validation.cif.gz | 17.9 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-37969 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-37969 | HTTPS FTP |
-Related structure data
Related structure data | 8x03MC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_37969.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.0975 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_37969_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_37969_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Structure of mitochondrial soluble protein
Entire | Name: Structure of mitochondrial soluble protein |
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Components |
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-Supramolecule #1: Structure of mitochondrial soluble protein
Supramolecule | Name: Structure of mitochondrial soluble protein / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Sus scrofa (pig) |
-Macromolecule #1: Acetyltransferase component of pyruvate dehydrogenase complex
Macromolecule | Name: Acetyltransferase component of pyruvate dehydrogenase complex type: protein_or_peptide / ID: 1 / Number of copies: 60 / Enantiomer: LEVO |
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Source (natural) | Organism: Sus scrofa (pig) |
Molecular weight | Theoretical: 69.262477 KDa |
Sequence | String: MWRVCARRAQ NAAPRAGFGA RWTALREEPG APCAAPRAGS VPARCSSTTR GYGRSRALCG WSASSWATPQ NRILLQLWGS PNRRWYSLP PHQKVPLPSL SPTMQAGTIA RWEKKEGDKI NEGELIAEVE TDKATVGFES LEECYMAKIL VAEGTRDVPV G AIICITVE ...String: MWRVCARRAQ NAAPRAGFGA RWTALREEPG APCAAPRAGS VPARCSSTTR GYGRSRALCG WSASSWATPQ NRILLQLWGS PNRRWYSLP PHQKVPLPSL SPTMQAGTIA RWEKKEGDKI NEGELIAEVE TDKATVGFES LEECYMAKIL VAEGTRDVPV G AIICITVE KPEDIEAFKN YTLDSSAAPA PQAAPAPTPA AAAPAPTPSA QAPGSSYPTH MQVVLPALSP TMTMGTVQRW EK KVGEKLS EGDLLAEIET DKATIGFEVQ EEGYLAKILI PEGTRDVPLG TPLCIIVEKE ADIPAFADYR PTEVTDLKPP APP PTPSPV TPVPPAPQPV APTPAATRPA TPAGPKGRLF VSPLAKKLAS EKGIDLTQIK GTGPDGRIIK KDIDSFVPTK AAPT PAAAV PPPSPGVAPV PTGVFTDIPI SNIRRVIAQR LMQSKQTIPH YYLSVDVNMG EVLLVRKELN KMLEGRSKIS VNDFI IKAS ALACLKVPEA NSSWLDTVIR QNHVVDISVA VSTPAGLITP IVFNAHIKGL ETIANDVVSL ATKAREGKLQ PHEFQG GTF TISNLGMFGI KNFSAIINPP QACILAVGAS EDRLFPADNE KGFDVASMMS VTLSCDHRVV DGAVGAQWLA EFRKYLE KP ITMLL UniProtKB: Acetyltransferase component of pyruvate dehydrogenase complex |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.8 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.66 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 35220 |
Initial angle assignment | Type: ANGULAR RECONSTITUTION |
Final angle assignment | Type: ANGULAR RECONSTITUTION |