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Yorodumi- EMDB-64136: Cryo-EM structure of the Pma1 with ordered N-terminal extension i... -
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Basic information
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| Title | Cryo-EM structure of the Pma1 with ordered N-terminal extension in the autoinhibited state | |||||||||
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Keywords | Autoinhibited state / PROTON TRANSPORT | |||||||||
| Function / homology | Function and homology informationP-type H+-exporting transporter / eisosome / proton export across plasma membrane / proteasome storage granule assembly / P-type proton-exporting transporter activity / positive regulation of TORC1 signaling / proton transmembrane transport / regulation of intracellular pH / transmembrane transport / membrane raft ...P-type H+-exporting transporter / eisosome / proton export across plasma membrane / proteasome storage granule assembly / P-type proton-exporting transporter activity / positive regulation of TORC1 signaling / proton transmembrane transport / regulation of intracellular pH / transmembrane transport / membrane raft / ATP hydrolysis activity / mitochondrion / ATP binding / metal ion binding / plasma membrane / cytosol Similarity search - Function | |||||||||
| Biological species | ![]() ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.52 Å | |||||||||
Authors | You ZL / Bai L | |||||||||
| Funding support | China, 1 items
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Citation | Journal: To Be PublishedTitle: Cryo-EM structure of the Pma1 with ordered N-terminal extension in the autoinhibited state Authors: You ZL / Bai L | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_64136.map.gz | 97.1 MB | EMDB map data format | |
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| Header (meta data) | emd-64136-v30.xml emd-64136.xml | 14.3 KB 14.3 KB | Display Display | EMDB header |
| Images | emd_64136.png | 76.2 KB | ||
| Filedesc metadata | emd-64136.cif.gz | 5.5 KB | ||
| Others | emd_64136_half_map_1.map.gz emd_64136_half_map_2.map.gz | 95.6 MB 95.7 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-64136 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-64136 | HTTPS FTP |
-Validation report
| Summary document | emd_64136_validation.pdf.gz | 833.2 KB | Display | EMDB validaton report |
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| Full document | emd_64136_full_validation.pdf.gz | 832.8 KB | Display | |
| Data in XML | emd_64136_validation.xml.gz | 13.4 KB | Display | |
| Data in CIF | emd_64136_validation.cif.gz | 15.9 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-64136 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-64136 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9ugcMC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_64136.map.gz / Format: CCP4 / Size: 103 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: 1.029 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_64136_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_64136_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Cryo-EM structure of the Pma1 with ordered N-terminal extension i...
| Entire | Name: Cryo-EM structure of the Pma1 with ordered N-terminal extension in the autoinhibited state |
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| Components |
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-Supramolecule #1: Cryo-EM structure of the Pma1 with ordered N-terminal extension i...
| Supramolecule | Name: Cryo-EM structure of the Pma1 with ordered N-terminal extension in the autoinhibited state type: cell / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Plasma membrane ATPase 1
| Macromolecule | Name: Plasma membrane ATPase 1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: P-type H+-exporting transporter |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 99.714023 KDa |
| Sequence | String: MTDTSSSSSS SSASSVSAHQ PTQEKPAKTY DDAASESSDD DDIDALIEEL QSNHGVDDED SDNDGPVAAG EARPVPEEYL QTDPSYGLT SDEVLKRRKK YGLNQMADEK ESLVVKFVMF FVGPIQFVME AAAILAAGLS DWVDFGVICG LLMLNAGVGF V QEFQAGSI ...String: MTDTSSSSSS SSASSVSAHQ PTQEKPAKTY DDAASESSDD DDIDALIEEL QSNHGVDDED SDNDGPVAAG EARPVPEEYL QTDPSYGLT SDEVLKRRKK YGLNQMADEK ESLVVKFVMF FVGPIQFVME AAAILAAGLS DWVDFGVICG LLMLNAGVGF V QEFQAGSI VDELKKTLAN TAVVIRDGQL VEIPANEVVP GDILQLEDGT VIPTDGRIVT EDCFLQIDQS AITGESLAVD KH YGDQTFS SSTVKRGEGF MVVTATGDNT FVGRAAALVN KAAGGQGHFT EVLNGIGIIL LVLVIATLLL VWTACFYRTN GIV RILRYT LGITIIGVPV GLPAVVTTTM AVGAAYLAKK QAIVQKLSAI ESLAGVEILC SDKTGTLTKN KLSLHEPYTV EGVS PDDLM LTACLAASRK KKGLDAIDKA FLKSLKQYPK AKDALTKYKV LEFHPFDPVS KKVTAVVESP EGERIVCVKG APLFV LKTV EEDHPIPEDV HENYENKVAE LASRGFRALG VARKRGEGHW EILGVMPCMD PPRDDTAQTV SEARHLGLRV KMLTGD AVG IAKETCRQLG LGTNIYNAER LGLGGGGDMP GSELADFVEN ADGFAEVFPQ HKYRVVEILQ NRGYLVAMTG DGVNDAP SL KKADTGIAVE GATDAARSAA DIVFLAPGLS AIIDALKTSR QIFHRMYSYV VYRIALSLHL EIFLGLWIAI LDNSLDID L IVFIAIFADV ATLAIAYDNA PYSPKPVKWN LPRLWGMSII LGIVLAIGSW ITLTTMFLPK GGIIQNFGAM NGIMFLQIS LTENWLIFIT RAAGPFWSSI PSWQLAGAVF AVDIIATMFT LFGWWSENWT DIVTVVRVWI WSIGIFCVLG GFYYEMSTSE AFDRLMNGK PMKEKKSTRS VEDFMAAMQR VSTQHEKET UniProtKB: Plasma membrane ATPase 1 |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.4 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TECNAI F30 |
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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: 1.8 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Tecnai F30 / Image courtesy: FEI Company |
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Keywords
Authors
China, 1 items
Citation



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Processing
FIELD EMISSION GUN
