Current Protein Identity:A0A5J6DWG4
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Difference tags compare only the current result set; every original PDB and assembly record remains separate.
Related-Structure Differences
Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.
| PDB Entry | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Experimental Method | Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 9YC9 HSV replication fork complex bound to pritelivir Deposited 2025-09-18 | Assembly 1 Protein–DNA Heteromer;Protein × 5 PDB declaration: octameric(8) Consistent with all polymers |
Chain C
1–1058(1058 aa)
|
Not recorded | ZN ZINC ION × 1 A1BXB Pritelivir × 1 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.80 Å |
| 9YCP HSV Helicase-primase complex bound to IM-250 Deposited 2025-09-19 | Assembly 1 Protein–DNA Heteromer;Protein × 3 PDB declaration: tetrameric(4) Consistent with all polymers |
Chain C
1–1058(1058 aa)
|
Not recorded | ZN ZINC ION × 1 A1CHB N-{5-[(R)-amino(hydroxy)(methyl)-lambda~4~-sulfanyl]-4-methyl-1,3-thiazol-2-yl}-2-(2',5'-difluoro[1,1'-biphenyl]-4-yl)-N-methylacetamide × 1 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.90 Å |
| 9YCT HSV helicase-primase complex bound to pritelivir Deposited 2025-09-19 | Assembly 1 Protein–DNA Heteromer;Protein × 3 PDB declaration: tetrameric(4) Consistent with all polymers |
Chain C
1–1058(1058 aa)
|
Not recorded | ZN ZINC ION × 1 A1BXB Pritelivir × 1 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.70 Å |
| 9YCV HSV Helicase-primase complex bound to amenamevir Deposited 2025-09-19 | Assembly 1 Protein–DNA Heteromer;Protein × 3 PDB declaration: tetrameric(4) Consistent with all polymers |
Chain C
1–1058(1058 aa)
|
Not recorded | ZN ZINC ION × 1 A1BXD Amenamevir × 1 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.80 Å |