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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | HBsAg in complex with H020 Fab | |||||||||
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Sample |
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Keywords | HBV / HBsAg / Fab / Antigentic loop / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex | |||||||||
| Function / homology | Large envelope protein S / Major surface antigen from hepadnavirus / membrane fusion involved in viral entry into host cell / symbiont entry into host cell / virion attachment to host cell / virion membrane / membrane / Middle S protein Function and homology information | |||||||||
| Biological species | ![]() Hepatitis B virus / Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.86 Å | |||||||||
Authors | Chen L / Tao W / He X | |||||||||
| Funding support | China, 1 items
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Citation | Journal: J Mol Biol / Year: 2025Title: The Symmetric Structure of the Antigenic Loop in Type B HBV Surface Antigen. Authors: Weiyu Tao / Xiao He / Lei Chen / ![]() Abstract: Hepatitis B virus (HBV) is an enveloped virus with HBV surface antigen (HBsAg) as the only protein on its viral membrane. The extracellular antigenic loop (AGL) of HBsAg plays a crucial role in viral ...Hepatitis B virus (HBV) is an enveloped virus with HBV surface antigen (HBsAg) as the only protein on its viral membrane. The extracellular antigenic loop (AGL) of HBsAg plays a crucial role in viral attachment to host cells, serves as the primary target for neutralizing antibodies (NAbs), and is subject to escape mutations. Previous studies have shown that the AGL exhibits two different structures (Type A and Type B) dictated by distinct disulfide bond linkage. However, due to the flexibility of some regions in previous structure, the complete model of AGL and its symmetry remain elusive. Here, we present the cryo-EM structure of AGL in complex with the Fab fragment of the NAb H020. The complete structure of AGL reveals its two-fold symmetry and it can bind two Fab fragments simultaneously. Further analysis elucidates the underlying mechanism of pan-serotype neutralizing capability of H020 and how escape mutations hinder its binding. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_64014.map.gz | 117.2 MB | EMDB map data format | |
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| Header (meta data) | emd-64014-v30.xml emd-64014.xml | 19.2 KB 19.2 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_64014_fsc.xml | 10.6 KB | Display | FSC data file |
| Images | emd_64014.png | 47.7 KB | ||
| Masks | emd_64014_msk_1.map | 125 MB | Mask map | |
| Filedesc metadata | emd-64014.cif.gz | 5.8 KB | ||
| Others | emd_64014_additional_1.map.gz emd_64014_half_map_1.map.gz emd_64014_half_map_2.map.gz | 117.7 MB 115.9 MB 115.9 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-64014 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-64014 | HTTPS FTP |
-Validation report
| Summary document | emd_64014_validation.pdf.gz | 850.9 KB | Display | EMDB validaton report |
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| Full document | emd_64014_full_validation.pdf.gz | 850.4 KB | Display | |
| Data in XML | emd_64014_validation.xml.gz | 18.6 KB | Display | |
| Data in CIF | emd_64014_validation.cif.gz | 23.7 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-64014 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-64014 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9ubqMC 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_64014.map.gz / Format: CCP4 / Size: 125 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: 0.833 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_64014_msk_1.map | ||||||||||||
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| Density Histograms |
-Additional map: #1
| File | emd_64014_additional_1.map | ||||||||||||
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-Half map: #2
| File | emd_64014_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_64014_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Structure of the Hepatitis B virus envelope protein in complex wi...
| Entire | Name: Structure of the Hepatitis B virus envelope protein in complex with H020 Fab |
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| Components |
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-Supramolecule #1: Structure of the Hepatitis B virus envelope protein in complex wi...
| Supramolecule | Name: Structure of the Hepatitis B virus envelope protein in complex with H020 Fab type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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-Supramolecule #2: envelope protein
| Supramolecule | Name: envelope protein / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1 |
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| Source (natural) | Organism: ![]() Hepatitis B virus |
-Supramolecule #3: H020 Fab
| Supramolecule | Name: H020 Fab / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2-#3 |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Middle S protein
| Macromolecule | Name: Middle S protein / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() Hepatitis B virus |
| Molecular weight | Theoretical: 31.153318 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MQWNSTTFHQ TLQDPRVRGL YFPAGGSSSG AVNPVPTTAS PLSSIFSRIG DPALNMENIT SGFLGPLLVL QAGFFLLTRI LTIPQSLDS WWTSLNFLGG TTVCLGQNSQ SPTSNHSPTS CPPTCPGYRW MALRRFIIFL FILLLALIFL LVLLDYQGML P VCPLIPGS ...String: MQWNSTTFHQ TLQDPRVRGL YFPAGGSSSG AVNPVPTTAS PLSSIFSRIG DPALNMENIT SGFLGPLLVL QAGFFLLTRI LTIPQSLDS WWTSLNFLGG TTVCLGQNSQ SPTSNHSPTS CPPTCPGYRW MALRRFIIFL FILLLALIFL LVLLDYQGML P VCPLIPGS STTSTGPCRT CMTTAQGTSM YPSCCCTKPS DGNCTCIPIP SSWAFGKFLW EWASARFSWL SLLVPFVQWF VG LSPTVWL SVIWMMWYWG PSLYSILSPF LPLLPIFFAL WVYI UniProtKB: Middle S protein |
-Macromolecule #2: H020 Fab Heavy Chain
| Macromolecule | Name: H020 Fab Heavy Chain / 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: 23.662443 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: QVQLQESGPG LVRPSETLSL TCTVSGGSIS NDYWSWIRQP PGKGLEWIGQ IHSKGDTNYN PSLKSRVTIS VDTSKNQLSL KVRSVTAAD TAVYYCARHL YRYGYRNYFD YWGQGNLVTV SSAASTKGPS VFPLAPSSKS TSGGTAALGC LVKDYFPEPV T VSWNSGAL ...String: QVQLQESGPG LVRPSETLSL TCTVSGGSIS NDYWSWIRQP PGKGLEWIGQ IHSKGDTNYN PSLKSRVTIS VDTSKNQLSL KVRSVTAAD TAVYYCARHL YRYGYRNYFD YWGQGNLVTV SSAASTKGPS VFPLAPSSKS TSGGTAALGC LVKDYFPEPV T VSWNSGAL TSGVHTFPAV LQSSGLYSLS SVVTVPSSSL GTQTYICNVN HKPSNTKVDK RV |
-Macromolecule #3: H020 Fab Light Chain
| Macromolecule | Name: H020 Fab Light Chain / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 23.178699 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: DIQMTQSPSS VSASVGDRVT IACRASQGIS SGLAWYQQKP GKAPKLLIHA ASSLQSGVPS RFSGSESGTE FTLTISSLQP EDFATYYCQ QANSFPLTFG GGTKVEFKPR TVAAPSVFIF PPSDEQLKSG TASVVCLLNN FYPREAKVQW KVDNALQSGN S QESVTEQD ...String: DIQMTQSPSS VSASVGDRVT IACRASQGIS SGLAWYQQKP GKAPKLLIHA ASSLQSGVPS RFSGSESGTE FTLTISSLQP EDFATYYCQ QANSFPLTFG GGTKVEFKPR TVAAPSVFIF PPSDEQLKSG TASVVCLLNN FYPREAKVQW KVDNALQSGN S QESVTEQD SKDSTYSLSS TLTLSKADYE KHKVYACEVT HQGLSSPVTK SFNRGEC |
-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: 8 |
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| Vitrification | Cryogen name: ETHANE |
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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: 52.0 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: 1.8 µm / Nominal defocus min: 1.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




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




















































Processing
FIELD EMISSION GUN

