+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-35393 | |||||||||
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Title | Human SLC26A3 in the apo state | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Transporter / MEMBRANE PROTEIN | |||||||||
Function / homology | Function and homology information Defective SLC26A3 causes congenital secretory chloride diarrhea 1 (DIAR1) / Multifunctional anion exchangers / sulfate transmembrane transporter activity / oxalate transmembrane transporter activity / secondary active sulfate transmembrane transporter activity / intracellular pH elevation / chloride:bicarbonate antiporter activity / solute:inorganic anion antiporter activity / membrane hyperpolarization / bicarbonate transmembrane transporter activity ...Defective SLC26A3 causes congenital secretory chloride diarrhea 1 (DIAR1) / Multifunctional anion exchangers / sulfate transmembrane transporter activity / oxalate transmembrane transporter activity / secondary active sulfate transmembrane transporter activity / intracellular pH elevation / chloride:bicarbonate antiporter activity / solute:inorganic anion antiporter activity / membrane hyperpolarization / bicarbonate transmembrane transporter activity / monoatomic anion transport / chloride transmembrane transporter activity / sperm capacitation / monoatomic ion transport / cellular response to cAMP / sperm midpiece / brush border membrane / apical plasma membrane / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
Authors | Li XR / Chi XM / Zhang YY / Zhou Q | |||||||||
Funding support | China, 1 items
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Citation | Journal: To Be Published Title: Human SLC26A3 in the apo state Authors: Li XR / Chi XM / Zhang YY / Zhou Q | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_35393.map.gz | 28.5 MB | EMDB map data format | |
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Header (meta data) | emd-35393-v30.xml emd-35393.xml | 13 KB 13 KB | Display Display | EMDB header |
Images | emd_35393.png | 51.9 KB | ||
Filedesc metadata | emd-35393.cif.gz | 5.3 KB | ||
Others | emd_35393_half_map_1.map.gz emd_35393_half_map_2.map.gz | 22.3 MB 22.3 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-35393 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-35393 | HTTPS FTP |
-Validation report
Summary document | emd_35393_validation.pdf.gz | 839.7 KB | Display | EMDB validaton report |
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Full document | emd_35393_full_validation.pdf.gz | 839.2 KB | Display | |
Data in XML | emd_35393_validation.xml.gz | 10.6 KB | Display | |
Data in CIF | emd_35393_validation.cif.gz | 12.4 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-35393 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-35393 | HTTPS FTP |
-Related structure data
Related structure data | 8ietMC 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_35393.map.gz / Format: CCP4 / Size: 30.5 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: 1.077 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_35393_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_35393_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Human SLC26A3 in the apo state
Entire | Name: Human SLC26A3 in the apo state |
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Components |
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-Supramolecule #1: Human SLC26A3 in the apo state
Supramolecule | Name: Human SLC26A3 in the apo state / type: cell / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Chloride anion exchanger
Macromolecule | Name: Chloride anion exchanger / 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: 84.591523 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: MIEPFGNQYI VARPVYSTNA FEENHKKTGR HHKTFLDHLK VCCSCSPQKA KRIVLSLFPI ASWLPAYRLK EWLLSDIVSG ISTGIVAVL QGLAFALLVD IPPVYGLYAS FFPAIIYLFF GTSRHISVGP FPILSMMVGL AVSGAVSKAV PDRNATTLGL P NNSNNSSL ...String: MIEPFGNQYI VARPVYSTNA FEENHKKTGR HHKTFLDHLK VCCSCSPQKA KRIVLSLFPI ASWLPAYRLK EWLLSDIVSG ISTGIVAVL QGLAFALLVD IPPVYGLYAS FFPAIIYLFF GTSRHISVGP FPILSMMVGL AVSGAVSKAV PDRNATTLGL P NNSNNSSL LDDERVRVAA AASVTVLSGI IQLAFGILRI GFVVIYLSES LISGFTTAAA VHVLVSQLKF IFQLTVPSHT DP VSIFKVL YSVFSQIEKT NIADLVTALI VLLVVSIVKE INQRFKDKLP VPIPIEFIMT VIAAGVSYGC DFKNRFKVAV VGD MNPGFQ PPITPDVETF QNTVGDCFGI AMVAFAVAFS VASVYSLKYD YPLDGNQELI ALGLGNIVCG VFRGFAGSTA LSRS AVQES TGGKTQIAGL IGAIIVLIVV LAIGFLLAPL QKSVLAALAL GNLKGMLMQF AEIGRLWRKD KYDCLIWIMT FIFTI VLGL GLGLAASVAF QLLTIVFRTQ FPKCSTLANI GRTNIYKNKK DYYDMYEPEG VKIFRCPSPI YFANIGFFRR KLIDAV GFS PLRILRKRNK ALRKIRKLQK QGLLQVTPKG FICTVDTIKD SDEELDNNQI EVLDQPINTT DLPFHIDWND DLPLNIE VP KISLHSLILD FSAVSFLDVS SVRGLKSILQ EFIRIKVDVY IVGTDDDFIE KLNRYEFFDG EVKSSIFFLT IHDAVLHI L MKKDYSTSKF NPSQEKDGKI DFTINTNGGL RNRVYEVPVE TKF UniProtKB: Chloride anion exchanger |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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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: 2.2 µm / Nominal defocus min: 1.2 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: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 142727 |
Initial angle assignment | Type: ANGULAR RECONSTITUTION |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |