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Open data
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Basic information
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| Title | Cryo-EM structure of human hyaluronidase PH-20 | |||||||||
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Keywords | hyaluronidase / endoglycosidase hydrolase / fab complex / HYDROLASE / HYDROLASE-IMMUNE SYSTEM complex | |||||||||
| Function / homology | Function and homology informationhyaluronoglucosaminidase / Interaction With Cumulus Cells And The Zona Pellucida / fusion of sperm to egg plasma membrane involved in single fertilization / hyalurononglucosaminidase activity / hyaluronan catabolic process / binding of sperm to zona pellucida / side of membrane / acrosomal vesicle / carbohydrate metabolic process / cell adhesion / plasma membrane Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) / ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.1 Å | |||||||||
Authors | Im S-B / Jeong T-K / Kim N / Oh B-H | |||||||||
| Funding support | Korea, Republic Of, 2 items
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Citation | Journal: Proteins / Year: 2025Title: Cryo-EM Structure of Human Hyaluronidase PH-20. Authors: Seong-Bin Im / Hyung Nam Song / Tae-Kyeong Jeong / Nayun Kim / Kyuwan Kim / Soon-Jae Park / Byung-Ha Oh / ![]() Abstract: PH-20 is a specific type of hyaluronidase that plays a critical role in the fertilization process by facilitating the initial binding of sperm to the glycoprotein layer surrounding the oocyte and ...PH-20 is a specific type of hyaluronidase that plays a critical role in the fertilization process by facilitating the initial binding of sperm to the glycoprotein layer surrounding the oocyte and subsequently breaking down hyaluronic acid polymers in the cumulus cell layer. PH-20 contains an epidermal growth factor (EGF)-like domain, which may be involved in the recognition of the glycoprotein layer in addition to the catalytic domain. Herein, we report the structure of human PH-20 determined by cryogenic electron microscopy. Comparative analyses of the PH-20 structure with two other available hyaluronidase structures reveal a general similarity in the central catalytic domains, including the conservation of catalytically essential residues at the equivalent spatial positions. However, unique difference is found in the EGF-like domain, characterized by a longer sequence that is likely to form a flexibly anchored β-hairpin containing a disulfide bond. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_61826.map.gz | 229.9 MB | EMDB map data format | |
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| Header (meta data) | emd-61826-v30.xml emd-61826.xml | 20.6 KB 20.6 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_61826_fsc.xml | 13.2 KB | Display | FSC data file |
| Images | emd_61826.png | 70.1 KB | ||
| Filedesc metadata | emd-61826.cif.gz | 6.4 KB | ||
| Others | emd_61826_half_map_1.map.gz emd_61826_half_map_2.map.gz | 226.4 MB 226.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-61826 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-61826 | HTTPS FTP |
-Validation report
| Summary document | emd_61826_validation.pdf.gz | 898.9 KB | Display | EMDB validaton report |
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| Full document | emd_61826_full_validation.pdf.gz | 898.5 KB | Display | |
| Data in XML | emd_61826_validation.xml.gz | 22.5 KB | Display | |
| Data in CIF | emd_61826_validation.cif.gz | 29 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-61826 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-61826 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9jubMC 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_61826.map.gz / Format: CCP4 / Size: 244.1 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: 0.664 Å | ||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_61826_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_61826_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Complex of human hyaluronidase PH-20 and 79C11Fab
| Entire | Name: Complex of human hyaluronidase PH-20 and 79C11Fab |
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| Components |
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-Supramolecule #1: Complex of human hyaluronidase PH-20 and 79C11Fab
| Supramolecule | Name: Complex of human hyaluronidase PH-20 and 79C11Fab / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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| Molecular weight | Theoretical: 90 KDa |
-Supramolecule #2: hyaluronidase PH-20
| Supramolecule | Name: hyaluronidase PH-20 / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1 |
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| Source (natural) | Organism: Homo sapiens (human) |
-Supramolecule #3: 79C11Fab
| Supramolecule | Name: 79C11Fab / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2-#3 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Hyaluronidase PH-20
| Macromolecule | Name: Hyaluronidase PH-20 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: hyaluronoglucosaminidase |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 46.610211 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: NFRAPPVIPN VPFLWAWNAP SEFCLGKFDE PLDMSLFSFI GSPRINATGQ GVTIFYVDRL GYYPYIDSIT GVTVNGGIPQ KISLQDHLD KAKKDITFYM PVDNLGMAVI DWEEWRPTWA RNWKPKDVYK NRSIELVQQQ NVQLSLTEAT EKAKQEFEKA G KDFLVETI ...String: NFRAPPVIPN VPFLWAWNAP SEFCLGKFDE PLDMSLFSFI GSPRINATGQ GVTIFYVDRL GYYPYIDSIT GVTVNGGIPQ KISLQDHLD KAKKDITFYM PVDNLGMAVI DWEEWRPTWA RNWKPKDVYK NRSIELVQQQ NVQLSLTEAT EKAKQEFEKA G KDFLVETI KLGKLLRPNH LWGYYLFPDC YNHHYKKPGY NGSCFNVEIK RNDDLSWLWN ESTALYPSIY LNTQQSPVAA TL YVRNRVR EAIRVSKIPD AKSPLPVFAY TRIVFTDQVL KFLSQDELVY TFGETVALGA SGIVIWGTLS IMRSMKSCLL LDN YMETIL NPYIINVTLA AKMCSQVLCQ EQGVCIRKNW NSSDYLHLNP DNFAIQLEKG GKFTVRGKPT LEDLEQFSEK FYCS CYSTL S UniProtKB: Hyaluronidase PH-20 |
-Macromolecule #2: Heavy chain of 79C11Fab
| Macromolecule | Name: Heavy chain of 79C11Fab / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 22.664252 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: QSVEESGGRL VTPGGSLTLT CTVSGFSLSS NAISWVRQAP GKGLEYIGII STSGSTYYAN WAKGRFTISK TSTTVDLKMT SLTTEDTAT YFCARDGAYD DFAYYFDLWG QGTLVTVSSG QPKAPSVFPL APCCGDTPSS TVTLGCLVKG YLPEPVTVTW N SGTLTNGV ...String: QSVEESGGRL VTPGGSLTLT CTVSGFSLSS NAISWVRQAP GKGLEYIGII STSGSTYYAN WAKGRFTISK TSTTVDLKMT SLTTEDTAT YFCARDGAYD DFAYYFDLWG QGTLVTVSSG QPKAPSVFPL APCCGDTPSS TVTLGCLVKG YLPEPVTVTW N SGTLTNGV RTFPSVRQSS GLYSLSSVVS VTSSSQPVTC NVAHPATNTK VDKTVAPS |
-Macromolecule #3: Light chain of 79C11Fab
| Macromolecule | Name: Light chain of 79C11Fab / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 22.270688 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: ALVMTQTPSS VSAAVGGTVT INCQASQNIY SGLAWYQQKL GQPPKLLIYK ASTLASGVPS RFKGSGSGTQ FTLTISGVQC DDAATYYCQ LAYSSTNVDN AFGGGTEVVV KGDPVAPTVL IFPPAADQVA TGTVTIVCVA NKYFPDVTVT WEVDGTTQTT G IENSKTPQ ...String: ALVMTQTPSS VSAAVGGTVT INCQASQNIY SGLAWYQQKL GQPPKLLIYK ASTLASGVPS RFKGSGSGTQ FTLTISGVQC DDAATYYCQ LAYSSTNVDN AFGGGTEVVV KGDPVAPTVL IFPPAADQVA TGTVTIVCVA NKYFPDVTVT WEVDGTTQTT G IENSKTPQ NSADCTYNLS STLTLTSTQY NSHKEYTCKV TQGTTSVVQS FNRG |
-Macromolecule #5: 2-acetamido-2-deoxy-beta-D-glucopyranose
| Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 5 / Number of copies: 3 / Formula: NAG |
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| Molecular weight | Theoretical: 221.208 Da |
| Chemical component information | ![]() ChemComp-NAG: |
-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 | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 69.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.3000000000000003 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Homo sapiens (human)
Authors
Korea, Republic Of, 2 items
Citation
Z (Sec.)
Y (Row.)
X (Col.)





































Processing
FIELD EMISSION GUN

