Coat protein
OrganismNot specified
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Protein homooligomer Homooligomer Protein × 120 PDB declaration: 120-meric（120） Consistent with protein copy count | Chain A； UniProt 274–1139 Chain B； UniProt 274–1139 | Not recorded | No other associated polymer | ELECTRON MICROSCOPY cryo-EM buffer：pH 9 cryo-EM vitrification conditions：Cryogen ETHANE；Grids were plunge-frozen using an EM GP2 (Leica Microsystems). The blotting arm height and position were adjusted, and a contact sensor was used to ensure reproducible blotting conditions. | Resolution 2.60 Å |
| 2 | Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count | Chain A； UniProt 274–1139 Chain B； UniProt 274–1139 | Not recorded | No other associated polymer | ELECTRON MICROSCOPY cryo-EM buffer：pH 9 cryo-EM vitrification conditions：Cryogen ETHANE；Grids were plunge-frozen using an EM GP2 (Leica Microsystems). The blotting arm height and position were adjusted, and a contact sensor was used to ensure reproducible blotting conditions. | Resolution 2.60 Å |
| 3 | Protein homooligomer Homooligomer Protein × 10 PDB declaration: decameric（10） Consistent with protein copy count | Chain A； UniProt 274–1139 Chain B； UniProt 274–1139 | Not recorded | No other associated polymer | ELECTRON MICROSCOPY cryo-EM buffer：pH 9 cryo-EM vitrification conditions：Cryogen ETHANE；Grids were plunge-frozen using an EM GP2 (Leica Microsystems). The blotting arm height and position were adjusted, and a contact sensor was used to ensure reproducible blotting conditions. | Resolution 2.60 Å |
| 4 | Protein homooligomer Homooligomer Protein × 12 PDB declaration: dodecameric（12） Consistent with protein copy count | Chain A； UniProt 274–1139 Chain B； UniProt 274–1139 | Not recorded | No other associated polymer | ELECTRON MICROSCOPY cryo-EM buffer：pH 9 cryo-EM vitrification conditions：Cryogen ETHANE；Grids were plunge-frozen using an EM GP2 (Leica Microsystems). The blotting arm height and position were adjusted, and a contact sensor was used to ensure reproducible blotting conditions. | Resolution 2.60 Å |
| 5 | Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count | Chain A； UniProt 274–1139 Chain B； UniProt 274–1139 | Not recorded | No other associated polymer | ELECTRON MICROSCOPY cryo-EM buffer：pH 9 cryo-EM vitrification conditions：Cryogen ETHANE；Grids were plunge-frozen using an EM GP2 (Leica Microsystems). The blotting arm height and position were adjusted, and a contact sensor was used to ensure reproducible blotting conditions. | Resolution 2.60 Å |
Other States of the Same Protein in the Database
Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.
No other PDB entry for the same UniProt protein was found.
View Construct and Data Evidence
| UniProt name | A0A172JTY4_9VIRU |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–866； UniProt 274–1139 Author chain B； PDBConstruct 1–866； UniProt 274–1139 |
