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Yorodumi- EMDB-32971: Structure of a human NHE3-CHP1 complex in the autoinhibited state -
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Basic information
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| Title | Structure of a human NHE3-CHP1 complex in the autoinhibited state | |||||||||
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Sample |
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Keywords | Sodium/proton antiporter / MEMBRANE PROTEIN | |||||||||
| Function / homology | Function and homology informationnegative regulation of phosphatase activity / positive regulation of sodium:proton antiporter activity / Sodium/Proton exchangers / Hyaluronan degradation / : / membrane docking / positive regulation of protein transport / negative regulation of protein autophosphorylation / transporter complex / positive regulation of phospholipid biosynthetic process ...negative regulation of phosphatase activity / positive regulation of sodium:proton antiporter activity / Sodium/Proton exchangers / Hyaluronan degradation / : / membrane docking / positive regulation of protein transport / negative regulation of protein autophosphorylation / transporter complex / positive regulation of phospholipid biosynthetic process / potassium:proton antiporter activity / sodium:proton antiporter activity / membrane organization / microtubule bundle formation / cellular response to acidic pH / sodium ion import across plasma membrane / negative regulation of calcineurin-NFAT signaling cascade / negative regulation of protein import into nucleus / small GTPase-mediated signal transduction / negative regulation of NF-kappaB transcription factor activity / endoplasmic reticulum-Golgi intermediate compartment / negative regulation of protein phosphorylation / protein kinase inhibitor activity / brush border / positive regulation of protein targeting to membrane / potassium channel regulator activity / negative regulation of protein kinase activity / transport vesicle / monoatomic ion transport / cytoplasmic microtubule organization / negative regulation of protein ubiquitination / potassium ion transmembrane transport / phosphatidylinositol binding / protein export from nucleus / regulation of intracellular pH / PDZ domain binding / brush border membrane / potassium ion transport / kinase binding / recycling endosome membrane / calcium-dependent protein binding / microtubule cytoskeleton / early endosome membrane / microtubule binding / membrane fusion / early endosome / protein stabilization / apical plasma membrane / membrane raft / Golgi membrane / focal adhesion / calcium ion binding / cell surface / endoplasmic reticulum / extracellular exosome / identical protein binding / nucleus / plasma membrane / cytoplasm Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||
Authors | Dong Y / Li H / Gao Y / Zhang XC / Zhao Y | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Sci Adv / Year: 2022Title: Structure of a human NHE3-CHP1 complex in the autoinhibited state Authors: Dong Y / Li H / Ilie A / Gao Y / Boucher A / Zhang XC / Orlowski J / Zhao Y | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_32971.map.gz | 5.6 MB | EMDB map data format | |
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| Header (meta data) | emd-32971-v30.xml emd-32971.xml | 14.1 KB 14.1 KB | Display Display | EMDB header |
| Images | emd_32971.png | 94.6 KB | ||
| Filedesc metadata | emd-32971.cif.gz | 6.2 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-32971 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-32971 | HTTPS FTP |
-Validation report
| Summary document | emd_32971_validation.pdf.gz | 376.4 KB | Display | EMDB validaton report |
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| Full document | emd_32971_full_validation.pdf.gz | 375.9 KB | Display | |
| Data in XML | emd_32971_validation.xml.gz | 5.3 KB | Display | |
| Data in CIF | emd_32971_validation.cif.gz | 6.2 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-32971 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-32971 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7x2uMC 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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Map
| File | Download / File: emd_32971.map.gz / Format: CCP4 / Size: 64 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 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : Human NHE3-CHP1 complex
| Entire | Name: Human NHE3-CHP1 complex |
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| Components |
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-Supramolecule #1: Human NHE3-CHP1 complex
| Supramolecule | Name: Human NHE3-CHP1 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Sodium/hydrogen exchanger 3
| Macromolecule | Name: Sodium/hydrogen exchanger 3 / 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: 70.537031 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: GGFQVVTFEW AHVQDPYVIA LWILVASLAK IGFHLSHKVT SVVPESALLI VLGLVLGGIV WAADHIASFT LTPTVFFFYL LPPIVLDAG YFMPNRLFFG NLGTILLYAV VGTVWNAATT GLSLYGVFLS GLMGDLQIGL LDFLLFGSLM AAVDPVAVLA V FEEVHVNE ...String: GGFQVVTFEW AHVQDPYVIA LWILVASLAK IGFHLSHKVT SVVPESALLI VLGLVLGGIV WAADHIASFT LTPTVFFFYL LPPIVLDAG YFMPNRLFFG NLGTILLYAV VGTVWNAATT GLSLYGVFLS GLMGDLQIGL LDFLLFGSLM AAVDPVAVLA V FEEVHVNE VLFIIVFGES LLNDAVTVVL YNVFESFVAL GGDNVTGVDC VKGIVSFFVV SLGGTLVGVV FAFLLSLVTR FT KHVRIIE PGFVFIISYL SYLTSEMLSL SAILAITFCG ICCQKYVKAN ISEQSATTVR YTMKMLASSA ETIIFMFLGI SAV NPFIWT WNTAFVLLTL VFISVYRAIG VVLQTWLLNR YRMVQLEPID QVVLSYGGLR GAVAFALVVL LDGDKVKEKN LFVS TTIIV VFFTVIFQGL TIKPLVQWLK VKRSEHREPR LNEKLHGRAF DHILSAIEDI SGQIGHNYLR DKWSHFDRKF LSRVL MRRS AQKSRDRILN VFHELNLKDA ISYVAEGERR GSLAFIRSPS TDNVVNVDFT PRSSTVEASV SYLLRENVSA VCLDMQ SLE QRRRSIRDAE DMVTHHTLQQ YLYKPRQEYK HLYSRHELTP TEDEKQDREI FHRTMRKRLE SFK UniProtKB: Sodium/hydrogen exchanger 3 |
-Macromolecule #2: Calcineurin B homologous protein 1
| Macromolecule | Name: Calcineurin B homologous protein 1 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 21.41191 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: DEELEEIKKE TGFSHSQITR LYSRFTSLDK GENGTLSRED FQRIPELAIN PLGDRIINAF FPEGEDQVNF RGFMRTLAHF RPIEDNEKS KDVNGPEPLN SRSNKLHFAF RLYDLDKDEK ISRDELLQVL RMMVGVNISD EQLGSIADRT IQEADQDGDS I ASFTEFVK VLEKVDVEQK MSIRFLH UniProtKB: Calcineurin B homologous protein 1 |
-Macromolecule #3: [(2~{R})-2-hexadecanoyloxy-3-[oxidanyl-[(2~{S},3~{S},5~{R},6~{S})...
| Macromolecule | Name: [(2~{R})-2-hexadecanoyloxy-3-[oxidanyl-[(2~{S},3~{S},5~{R},6~{S})-2,3,4,5,6-pentakis(oxidanyl)cyclohexyl]oxy-phosphoryl]oxy-propyl] hexadecanoate type: ligand / ID: 3 / Number of copies: 2 / Formula: 85R |
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| Molecular weight | Theoretical: 811.032 Da |
| Chemical component information | ![]() ChemComp-85R: |
-Macromolecule #4: (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-...
| Macromolecule | Name: (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE type: ligand / ID: 4 / Number of copies: 10 / Formula: PGT |
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| Molecular weight | Theoretical: 751.023 Da |
| Chemical component information | ![]() ChemComp-PGT: |
-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: 7.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 60.0 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: 22.0 µm / Nominal defocus min: 12.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Homo sapiens (human)
Authors
China, 1 items
Citation
Z (Sec.)
Y (Row.)
X (Col.)






















Processing
FIELD EMISSION GUN

