+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-39460 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Structure of HKU1A RBD with TMPRSS2 | |||||||||
Map data | ||||||||||
Sample |
| |||||||||
Keywords | HKU1A / RBD / TMPRSS2 / VIRAL PROTEIN/HYDROLASE / VIRAL PROTEIN-HYDROLASE complex | |||||||||
Function / homology | Function and homology information transmembrane protease serine 2 / protein autoprocessing / Attachment and Entry / serine-type peptidase activity / endocytosis involved in viral entry into host cell / viral translation / Induction of Cell-Cell Fusion / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / Attachment and Entry / positive regulation of viral entry into host cell ...transmembrane protease serine 2 / protein autoprocessing / Attachment and Entry / serine-type peptidase activity / endocytosis involved in viral entry into host cell / viral translation / Induction of Cell-Cell Fusion / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / Attachment and Entry / positive regulation of viral entry into host cell / receptor-mediated virion attachment to host cell / fusion of virus membrane with host plasma membrane / serine-type endopeptidase activity / fusion of virus membrane with host endosome membrane / viral envelope / host cell plasma membrane / virion membrane / proteolysis / extracellular exosome / extracellular region / nucleoplasm / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) / Candidatus Accumulibacter adiacens (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.21 Å | |||||||||
Authors | Gao X / Cui S / Ding W / Shang K / Zhu H / Zhu K | |||||||||
Funding support | 1 items
| |||||||||
Citation | Journal: Cell Discov / Year: 2024 Title: Structural basis for the interaction between human coronavirus HKU1 spike receptor binding domain and its receptor TMPRSS2. Authors: Xiaopan Gao / Kaixiang Zhu / Lin Wang / Kun Shang / Lei Hua / Bo Qin / Hongtao Zhu / Wei Ding / Sheng Cui / | |||||||||
History |
|
-Structure visualization
Supplemental images |
---|
-Downloads & links
-EMDB archive
Map data | emd_39460.map.gz | 58 MB | EMDB map data format | |
---|---|---|---|---|
Header (meta data) | emd-39460-v30.xml emd-39460.xml | 15.7 KB 15.7 KB | Display Display | EMDB header |
Images | emd_39460.png | 44.6 KB | ||
Masks | emd_39460_msk_1.map | 115.9 MB | Mask map | |
Filedesc metadata | emd-39460.cif.gz | 6 KB | ||
Others | emd_39460_half_map_1.map.gz emd_39460_half_map_2.map.gz | 107.6 MB 107.6 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-39460 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-39460 | HTTPS FTP |
-Validation report
Summary document | emd_39460_validation.pdf.gz | 744.6 KB | Display | EMDB validaton report |
---|---|---|---|---|
Full document | emd_39460_full_validation.pdf.gz | 744.2 KB | Display | |
Data in XML | emd_39460_validation.xml.gz | 13.9 KB | Display | |
Data in CIF | emd_39460_validation.cif.gz | 16.2 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-39460 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-39460 | HTTPS FTP |
-Related structure data
Related structure data | 8yoyMC 8yqqC M: atomic model generated by this map C: citing same article (ref.) |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
---|---|
Related items in Molecule of the Month |
-Map
File | Download / File: emd_39460.map.gz / Format: CCP4 / Size: 115.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.81 Å | ||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Mask #1
File | emd_39460_msk_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #1
File | emd_39460_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #2
File | emd_39460_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Sample components
-Entire : HKU1A-RBD with TMPRSS2 receptor
Entire | Name: HKU1A-RBD with TMPRSS2 receptor |
---|---|
Components |
|
-Supramolecule #1: HKU1A-RBD with TMPRSS2 receptor
Supramolecule | Name: HKU1A-RBD with TMPRSS2 receptor / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
---|---|
Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Spike protein S1
Macromolecule | Name: Spike protein S1 / type: protein_or_peptide / ID: 1 Details: Sequence reference for Candidatus Accumulibacter adiacens (2954378) is not available in UniProt at the time of biocuration. Current sequence reference is from UniProt ID Q5MQD0. Number of copies: 1 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: Candidatus Accumulibacter adiacens (bacteria) |
Molecular weight | Theoretical: 41.425062 KDa |
Recombinant expression | Organism: Baculovirus expression vector pFastBac1-HM |
Sequence | String: SGFTVKPVAT VHRRIPDLPD CDIDKWLNNF NVPSPLNWER KIFSNCNFNL STLLRLVHTD SFSCNNFDES KIYGSCFKSI VLDKFAIPN SRRSDLQLGS SGFLQSSNYK IDTTSSSCQL YYSLPAINVT INNYNPSSWN RRYGFNNFNL SSHSVVYSRY C FSVNNTFC ...String: SGFTVKPVAT VHRRIPDLPD CDIDKWLNNF NVPSPLNWER KIFSNCNFNL STLLRLVHTD SFSCNNFDES KIYGSCFKSI VLDKFAIPN SRRSDLQLGS SGFLQSSNYK IDTTSSSCQL YYSLPAINVT INNYNPSSWN RRYGFNNFNL SSHSVVYSRY C FSVNNTFC PCAKPSFASS CKSHKPPSAS CPIGTNYRSC ESTTVLDHTD WCRCSCLPDP ITAYDPRSCS QKKSLVGVGE HC AGFGVDE EKCGVLDGSY NVSCLCSTDA FLGWSYDTCV SNNRCNIFSN FILNGINSGT TCSNDLLQPN TEVFTDVCVD YDL YGITGQ GIFKEVSAVY YNSWQNLLYD SNGNIIGFKD FVTNKTYNIF PCYAG UniProtKB: Spike glycoprotein |
-Macromolecule #2: Transmembrane protease serine 2
Macromolecule | Name: Transmembrane protease serine 2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: transmembrane protease serine 2 |
---|---|
Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 42.381848 KDa |
Recombinant expression | Organism: Baculovirus expression vector pFastBac1-HM |
Sequence | String: MGSKCSNSGI ECDSSGTCIN PSNWCDGVSH CPGGEDENRC VRLYGPNFIL QVYSSQRKSW HPVCQDDWNE NYGRAACRDM GYKNNFYSS QGIVDDSGST SFMKLNTSAG NVDIYKKLYH SDACSSKAVV SLRCIACGVN LNSSRQSRIV GGESALPGAW P WQVSLHVQ ...String: MGSKCSNSGI ECDSSGTCIN PSNWCDGVSH CPGGEDENRC VRLYGPNFIL QVYSSQRKSW HPVCQDDWNE NYGRAACRDM GYKNNFYSS QGIVDDSGST SFMKLNTSAG NVDIYKKLYH SDACSSKAVV SLRCIACGVN LNSSRQSRIV GGESALPGAW P WQVSLHVQ NVHVCGGSII TPEWIVTAAH CVEKPLNNPW HWTAFAGILR QSFMFYGAGY QVEKVISHPN YDSKTKNNDI AL MKLQKPL TFNDLVKPVC LPNPGMMLQP EQLCWISGWG ATEEKGKTSE VLNAAKVLLI ETQRCNSRYV YDNLITPAMI CAG FLQGNV DSCQGDAGGP LVTSKNNIWW LIGDTSWGSG CAKAYRPGVY GNVMVFTDWI YRQMRADG UniProtKB: Transmembrane protease serine 2 |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
---|---|
Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 55.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Calibrated defocus max: 2.5 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.8 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: NONE |
---|---|
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.21 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 423131 |
Initial angle assignment | Type: ANGULAR RECONSTITUTION |
Final angle assignment | Type: ANGULAR RECONSTITUTION |