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- EMDB-33471: Human SLC26A3 in complex with UK5099 -

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ID or keywords:

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Basic information

Entry
Database: EMDB / ID: EMD-33471
TitleHuman SLC26A3 in complex with UK5099
Map data
Sample
  • Cell: human SLC26A3 in complex with UK5099
    • Protein or peptide: Chloride anion exchanger
  • Ligand: (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid
  • Ligand: CHOLESTEROL HEMISUCCINATE
Function / homology
Function and homology information


Defective SLC26A3 causes congenital secretory chloride diarrhea 1 (DIAR1) / Multifunctional anion exchangers / oxalate transmembrane transporter activity / sulfate 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 / oxalate transmembrane transporter activity / sulfate 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
Sulphate anion transporter, conserved site / SLC26A transporters signature. / SLC26A/SulP transporter / SLC26A/SulP transporter domain / Sulfate permease family / STAS domain / STAS domain profile. / STAS domain / STAS domain superfamily
Similarity search - Domain/homology
Chloride anion exchanger
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.8 Å
AuthorsLi XR / Chi XM / Zhang YY / Zhou Q
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31971123 China
CitationJournal: To Be Published
Title: human SLC26A3 in complex with UK5099
Authors: Li XR / Chi XM / Zhang YY / Zhou Q
History
DepositionMay 18, 2022-
Header (metadata) releaseMay 24, 2023-
Map releaseMay 24, 2023-
UpdateMay 24, 2023-
Current statusMay 24, 2023Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_33471.png

Downloads & links

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Map

FileDownload / File: emd_33471.map.gz / Format: CCP4 / Size: 38.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.077 Å
Density
Contour LevelBy AUTHOR: 0.023
Minimum - Maximum-0.06883573 - 0.14561795
Average (Standard dev.)0.00047549023 (±0.0047089234)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions216216216
Spacing216216216
CellA=B=C: 232.632 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_33471_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_33471_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : human SLC26A3 in complex with UK5099

EntireName: human SLC26A3 in complex with UK5099
Components
  • Cell: human SLC26A3 in complex with UK5099
    • Protein or peptide: Chloride anion exchanger
  • Ligand: (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid
  • Ligand: CHOLESTEROL HEMISUCCINATE

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Supramolecule #1: human SLC26A3 in complex with UK5099

SupramoleculeName: human SLC26A3 in complex with UK5099 / type: cell / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Chloride anion exchanger

MacromoleculeName: Chloride anion exchanger / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 79.333672 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: QYIVARPVYS TNAFEENHKK TGRHHKTFLD HLKVCCSCSP QKAKRIVLSL FPIASWLPAY RLKEWLLSDI VSGISTGIVA VLQGLAFAL LVDIPPVYGL YASFFPAIIY LFFGTSRHIS VGPFPILSMM VGLAVSGAVS KAVPDRNATT LGLPNNSNNS S LLDDERVR ...String:
QYIVARPVYS TNAFEENHKK TGRHHKTFLD HLKVCCSCSP QKAKRIVLSL FPIASWLPAY RLKEWLLSDI VSGISTGIVA VLQGLAFAL LVDIPPVYGL YASFFPAIIY LFFGTSRHIS VGPFPILSMM VGLAVSGAVS KAVPDRNATT LGLPNNSNNS S LLDDERVR VAAAASVTVL SGIIQLAFGI LRIGFVVIYL SESLISGFTT AAAVHVLVSQ LKFIFQLTVP SHTDPVSIFK VL YSVFSQI EKTNIADLVT ALIVLLVVSI VKEINQRFKD KLPVPIPIEF IMTVIAAGVS YGCDFKNRFK VAVVGDMNPG FQP PITPDV ETFQNTVGDC FGIAMVAFAV AFSVASVYSL KYDYPLDGNQ ELIALGLGNI VCGVFRGFAG STALSRSAVQ ESTG GKTQI AGLIGAIIVL IVVLAIGFLL APLQKSVLAA LALGNLKGML MQFAEIGRLW RKDKYDCLIW IMTFIFTIVL GLGLG LAAS VAFQLLTIVF RTQFPKCSTL ANIGRTNIYK NKKDYYDMYE PEGVKIFRCP SPIYFANIGF FRRKLIDAVG FSPLRI LRK RNKALRKIRK LQKQGLLQVT PKGFICTVDT IKDSDEELDN NQIEVLDQPI NTTDLPFHID WNDDLPLNIE VPKISLH SL ILDFSAVSFL DVSSVRGLKS ILQEFIRIKV DVYIVGTDDD FIEKLNRYEF FDGEVKSSIF FLTIHDAVLH ILMKKD

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Macromolecule #2: (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid

MacromoleculeName: (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid / type: ligand / ID: 2 / Number of copies: 2 / Formula: I2R
Molecular weightTheoretical: 288.3 Da
Chemical component information

ChemComp-I2R:
(E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid

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Macromolecule #3: CHOLESTEROL HEMISUCCINATE

MacromoleculeName: CHOLESTEROL HEMISUCCINATE / type: ligand / ID: 3 / Number of copies: 8 / Formula: Y01
Molecular weightTheoretical: 486.726 Da
Chemical component information

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.2 µm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 2277517

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