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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | ATP-bound structure of P2X332 | |||||||||
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Sample |
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Keywords | P2X / SIGNALING PROTEIN | |||||||||
| Function / homology | Function and homology informationPlatelet homeostasis / extracellularly ATP-gated monoatomic cation channel activity / purinergic nucleotide receptor activity / Elevation of cytosolic Ca2+ levels / response to ATP / protein homotrimerization / cellular response to ATP / ligand-gated monoatomic ion channel activity / positive regulation of calcium ion transport into cytosol / response to ischemia ...Platelet homeostasis / extracellularly ATP-gated monoatomic cation channel activity / purinergic nucleotide receptor activity / Elevation of cytosolic Ca2+ levels / response to ATP / protein homotrimerization / cellular response to ATP / ligand-gated monoatomic ion channel activity / positive regulation of calcium ion transport into cytosol / response to ischemia / neuronal dense core vesicle / sensory perception of sound / positive regulation of calcium-mediated signaling / hippocampal mossy fiber to CA3 synapse / transmembrane transport / modulation of chemical synaptic transmission / Schaffer collateral - CA1 synapse / calcium ion transmembrane transport / postsynapse / signaling receptor complex / apical plasma membrane / axon / neuronal cell body / signal transduction / ATP binding / identical protein binding / plasma membrane Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.69 Å | |||||||||
Authors | Wang C / Yu Y | |||||||||
| Funding support | China, 1 items
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Citation | Journal: To Be PublishedTitle: Structure and gating mechanism of P2X2/P2X3 heteromer channels Authors: Wang C / Yu Y | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_66457.map.gz | 85.2 MB | EMDB map data format | |
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| Header (meta data) | emd-66457-v30.xml emd-66457.xml | 15.9 KB 15.9 KB | Display Display | EMDB header |
| Images | emd_66457.png | 96.2 KB | ||
| Filedesc metadata | emd-66457.cif.gz | 5.8 KB | ||
| Others | emd_66457_half_map_1.map.gz emd_66457_half_map_2.map.gz | 94.7 MB 94.6 MB | ||
| Archive directory | https://data.pdbj.org/pub/emdb/structures/EMD-66457 ftp://data.pdbj.org/pub/emdb/structures/EMD-66457 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9x1cMC ![]() 9x1aC ![]() 9x1bC ![]() 9x1dC 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_66457.map.gz / Format: CCP4 / Size: 103 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: 0.855 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_66457_half_map_1.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
-Half map: #1
| File | emd_66457_half_map_2.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : P2X332 ATP-bound form
| Entire | Name: P2X332 ATP-bound form |
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| Components |
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-Supramolecule #1: P2X332 ATP-bound form
| Supramolecule | Name: P2X332 ATP-bound form / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: P2X purinoceptor 2
| Macromolecule | Name: P2X purinoceptor 2 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 51.814996 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MAAAQPKYPA GATARRLARG CWSALWDYET PKVIVVRNRR LGVLYRAVQL LILLYFVWYV FIVQKSYQES ETGPESSIIT KVKGITTSE HKVWDVEEYV KPPEGGSVFS IITRVEATHS QTQGTCPESI RVHNATCLSD ADCVAGELDM LGNGLRTGRC V PYYQGPSK ...String: MAAAQPKYPA GATARRLARG CWSALWDYET PKVIVVRNRR LGVLYRAVQL LILLYFVWYV FIVQKSYQES ETGPESSIIT KVKGITTSE HKVWDVEEYV KPPEGGSVFS IITRVEATHS QTQGTCPESI RVHNATCLSD ADCVAGELDM LGNGLRTGRC V PYYQGPSK TCEVFGWCPV EDGASVSQFL GTMAPNFTIL IKNSIHYPKF HFSKGNIADR TDGYLKRCTF HEASDLYCPI FK LGFIVEK AGESFTELAH KGGVIGVIIN WDCDLDLPAS ECNPKYSFRR LDPKHVPASS GYNFRFAKYY KINGTTTRTL IKA YGIRID VIVHGQAGKF SLIPTIINLA TALTSVGVGS FLCDWILLTF MNKNKVYSHK KFDKVCTPSH PSGSWPVTLA RVLG QAPPE PGHRSEDQHP SPPSGQEGQQ GAECGPAFPP LRPCPISAPS EQMVDTPASE PAQASTPTDP KGLAQL UniProtKB: P2X purinoceptor 2 |
-Macromolecule #2: P2X purinoceptor 3
| Macromolecule | Name: P2X purinoceptor 3 / 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: 44.334824 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MNCISDFFTY ETTKSVVVKS WTIGIINRVV QLLIISYFVG WVFLHEKAYQ VRDTAIESSV VTKVKGSGLY ANRVMDVSDY VTPPQGTSV FVIITKMIVT ENQMQGFCPE SEEKYRCVSD SQCGPERLPG GGILTGRCVN YSSVLRTCEI QGWCPTEVDT V ETPIMMEA ...String: MNCISDFFTY ETTKSVVVKS WTIGIINRVV QLLIISYFVG WVFLHEKAYQ VRDTAIESSV VTKVKGSGLY ANRVMDVSDY VTPPQGTSV FVIITKMIVT ENQMQGFCPE SEEKYRCVSD SQCGPERLPG GGILTGRCVN YSSVLRTCEI QGWCPTEVDT V ETPIMMEA ENFTIFIKNS IRFPLFNFEK GNLLPNLTAR DMKTCRFHPD KDPFCPILRV GDVVKFAGQD FAKLARTGGV LG IKIGWVC DLDKAWDQCI PKYSFTRLDS VSEKSSVSPG YNFRFAKYYK MENGSEYRTL LKAFGIRFDV LVYGNAGKFN IIP TIISSV AAFTSVGVGT VLCDIILLNF LKGADQYKAK KFEEVNETTL KIAALTNPVY PSDQTTAEKQ STDSGAFSIG H UniProtKB: P2X purinoceptor 3 |
-Macromolecule #3: ADENOSINE-5'-TRIPHOSPHATE
| Macromolecule | Name: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 3 / Formula: ATP |
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| Molecular weight | Theoretical: 507.181 Da |
| Chemical component information | ![]() ChemComp-ATP: |
-Macromolecule #4: MAGNESIUM ION
| Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 4 / Number of copies: 2 / Formula: MG |
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| Molecular weight | Theoretical: 24.305 Da |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 6 mg/mL |
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| Buffer | pH: 7.5 |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 6 K |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 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






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Y (Row.)
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Processing
FIELD EMISSION GUN
