+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-30495 | |||||||||
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Title | Cryo-EM structure of human TMEM120A/TACAN | |||||||||
Map data | ||||||||||
Sample |
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Keywords | MEMBRANE PROTEIN | |||||||||
Function / homology | Function and homology information protein heterooligomerization / nuclear inner membrane / fat cell differentiation / bioluminescence / generation of precursor metabolites and energy / detection of mechanical stimulus involved in sensory perception of pain / monoatomic ion transmembrane transport / protein homooligomerization / monoatomic ion channel activity / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | Anaplasma marginale (bacteria) / Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
Authors | Yan Z / Wu J | |||||||||
Citation | Journal: Cell Discov / Year: 2021 Title: Cryo-EM structures of human TMEM120A and TMEM120B. Authors: Meng Ke / Yue Yu / Changjian Zhao / Shirong Lai / Qiang Su / Weidan Yuan / Lina Yang / Dong Deng / Kun Wu / Weizheng Zeng / Jia Geng / Jianping Wu / Zhen Yan / | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_30495.map.gz | 482.5 KB | EMDB map data format | |
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Header (meta data) | emd-30495-v30.xml emd-30495.xml | 15.6 KB 15.6 KB | Display Display | EMDB header |
Images | emd_30495.png | 97.2 KB | ||
Masks | emd_30495_msk_1.map | 40.6 MB | Mask map | |
Filedesc metadata | emd-30495.cif.gz | 5.3 KB | ||
Others | emd_30495_additional_1.map.gz emd_30495_half_map_1.map.gz emd_30495_half_map_2.map.gz | 3.5 MB 37.7 MB 37.7 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-30495 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-30495 | HTTPS FTP |
-Validation report
Summary document | emd_30495_validation.pdf.gz | 760.9 KB | Display | EMDB validaton report |
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Full document | emd_30495_full_validation.pdf.gz | 760.4 KB | Display | |
Data in XML | emd_30495_validation.xml.gz | 11.2 KB | Display | |
Data in CIF | emd_30495_validation.cif.gz | 13.1 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-30495 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-30495 | HTTPS FTP |
-Related structure data
Related structure data | 7cxrMC 7f73C M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_30495.map.gz / Format: CCP4 / Size: 40.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Voxel size | X=Y=Z: 1.087 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
File | emd_30495_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: #1
File | emd_30495_additional_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_30495_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_30495_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Homodimer of human TMEM120A
Entire | Name: Homodimer of human TMEM120A |
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Components |
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-Supramolecule #1: Homodimer of human TMEM120A
Supramolecule | Name: Homodimer of human TMEM120A / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Anaplasma marginale (bacteria) |
-Macromolecule #1: MCherry fluorescent protein,Ion channel TACAN
Macromolecule | Name: MCherry fluorescent protein,Ion channel TACAN / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 72.643555 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: MDYKDDDDKG SDYKDDDDKG SDYKDDDDKG SDEVDAMVSK GEEDNMAIIK EFMRFKVHME GSVNGHEFEI EGEGEGRPYE GTQTAKLKV TKGGPLPFAW DILSPQFMYG SKAYVKHPAD IPDYLKLSFP EGFKWERVMN FEDGGVVTVT QDSSLQDGEF I YKVKLRGT ...String: MDYKDDDDKG SDYKDDDDKG SDYKDDDDKG SDEVDAMVSK GEEDNMAIIK EFMRFKVHME GSVNGHEFEI EGEGEGRPYE GTQTAKLKV TKGGPLPFAW DILSPQFMYG SKAYVKHPAD IPDYLKLSFP EGFKWERVMN FEDGGVVTVT QDSSLQDGEF I YKVKLRGT NFPSDGPVMQ KKTMGWEASS ERMYPEDGAL KGEIKQRLKL KDGGHYDAEV KTTYKAKKPV QLPGAYNVNI KL DITSHNE DYTIVEQYER AEGRHSTGGM DELYKLEVLF QGPEFMQPPP PGPLGDCLRD WEDLQQDFQN IQETHRLYRL KLE ELTKLQ NNCTSSITRQ KKRLQELALA LKKCKPSLPA EAEGAAQELE NQMKERQGLF FDMEAYLPKK NGLYLSLVLG NVNV TLLSK QAKFAYKDEY EKFKLYLTII LILISFTCRF LLNSRVTDAA FNFLLVWYYC TLTIRESILI NNGSRIKGWW VFHHY VSTF LSGVMLTWPD GLMYQKFRNQ FLSFSMYQSF VQFLQYYYQS GCLYRLRALG ERHTMDLTVE GFQSWMWRGL TFLLPF LFF GHFWQLFNAL TLFNLAQDPQ CKEWQVLMCG FPFLLLFLGN FFTTLRVVHH KFHSQRHGSK KD UniProtKB: MCherry fluorescent protein, Ion channel TACAN |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
-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 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: NONE / Details: Ab Initio |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 79080 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |