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- EMDB-35089: Mouse Pendrin bound chloride in inward state -

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Basic information

Entry
Database: EMDB / ID: EMD-35089
TitleMouse Pendrin bound chloride in inward state
Map data
Sample
  • Complex: mouse Pendrin bound chloride in inward state
    • Protein or peptide: Pendrin
  • Ligand: CHLORIDE ION
Keywordsexchange / transport / slc / TRANSPORT PROTEIN
Function / homology
Function and homology information


Inorganic anion exchange by SLC26 transporters / iodide transmembrane transporter activity / secondary active sulfate transmembrane transporter activity / monoatomic anion transmembrane transporter activity / regulation of pH / chloride:bicarbonate antiporter activity / animal organ morphogenesis / brush border membrane / regulation of protein localization / apical plasma membrane ...Inorganic anion exchange by SLC26 transporters / iodide transmembrane transporter activity / secondary active sulfate transmembrane transporter activity / monoatomic anion transmembrane transporter activity / regulation of pH / chloride:bicarbonate antiporter activity / animal organ morphogenesis / brush border membrane / regulation of protein localization / apical plasma membrane / extracellular exosome / 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
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.25 Å
AuthorsLiu QY / Zhang X / Sun L / Chen ZG
CitationJournal: To Be Published
Title: Mouse Pendrin bound chloride in inward state
Authors: Liu QY / Zhang X / Sun L / Chen ZG
History
DepositionJan 9, 2023-
Header (metadata) releaseJan 31, 2024-
Map releaseJan 31, 2024-
UpdateSep 3, 2025-
Current statusSep 3, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_35089.png

Downloads & links

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Map

FileDownload / File: emd_35089.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.05 Å/pix.
x 320 pix.
= 334.72 Å		1.05 Å/pix.
x 320 pix.
= 334.72 Å		1.05 Å/pix.
x 320 pix.
= 334.72 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.046 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.01
Minimum - Maximum-0.004329605 - 1.6057756
Average (Standard dev.)0.0006531808 (±0.017737588)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 334.72 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_35089_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_35089_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 : mouse Pendrin bound chloride in inward state

EntireName: mouse Pendrin bound chloride in inward state
Components
  • Complex: mouse Pendrin bound chloride in inward state
    • Protein or peptide: Pendrin
  • Ligand: CHLORIDE ION

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Supramolecule #1: mouse Pendrin bound chloride in inward state

SupramoleculeName: mouse Pendrin bound chloride in inward state / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Mus musculus (house mouse)

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Macromolecule #1: Pendrin

MacromoleculeName: Pendrin / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 85.769578 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MAARGGRSEP PQLAEYSCSY TVSRPVYSEL AFQQQRERRL PERRTLRDSL ARSCSCSRKR AFGVVKTLLP ILDWLPKYRV KEWLLSDII SGVSTGLVGT LQGMAYALLA AVPVQFGLYS AFFPILTYFV FGTSRHISVG PFPVVSLMVG SVVLSMAPDD H FLVPSGNG ...String:
MAARGGRSEP PQLAEYSCSY TVSRPVYSEL AFQQQRERRL PERRTLRDSL ARSCSCSRKR AFGVVKTLLP ILDWLPKYRV KEWLLSDII SGVSTGLVGT LQGMAYALLA AVPVQFGLYS AFFPILTYFV FGTSRHISVG PFPVVSLMVG SVVLSMAPDD H FLVPSGNG SALNSTTLDT GTRDAARVLL ASTLTLLVGI IQLVFGGLQI GFIVRYLADP LVGGFTTAAA FQVLVSQLKI VL NVSTKNY NGILSIIYTL IEIFQNIGDT NIADFIAGLL TIIVCMAVKE LNDRFKHRIP VPIPIEVIVT IIATAISYGA NLE KNYNAG IVKSIPSGFL PPVLPSVGLF SDMLAASFSI AVVAYAIAVS VGKVYATKHD YVIDGNQEFI AFGISNVFSG FFSC FVATT ALSRTAVQES TGGKTQVAGL ISAVIVMVAI VALGRLLEPL QKSVLAAVVI ANLKGMFMQV CDVPRLWKQN KTDAV IWVF TCIMSIILGL DLGLLAGLLF ALLTVVLRVQ FPSWNGLGSV PSTDIYKSIT HYKNLEEPEG VKILRFSSPI FYGNVD GFK KCINSTVGFD AIRVYNKRLK ALRRIQKLIK KGQLRATKNG IISDIGSSNN AFEPDEDVEE PEELNIPTKE IEIQVDW NS ELPVKVNVPK VPIHSLVLDC GAVSFLDVVG VRSLRMIVKE FQRIDVNVYF ALLQDDVLEK MEQCGFFDDN IRKDRFFL T VHDAILHLQN QVKSREGQDS LLETVARIRD CKDPLDLMEA EMNAEELDVQ DEAMRRLAS

UniProtKB: Pendrin

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Macromolecule #2: CHLORIDE ION

MacromoleculeName: CHLORIDE ION / type: ligand / ID: 2 / Number of copies: 2 / Formula: CL
Molecular weightTheoretical: 35.453 Da

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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: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 53.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.25 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 120887
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING

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