Major capsid protein VP1
Norovirus GII.4 Sydney 2012
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 heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count | Chain A; UniProt 221–530 Chain B; UniProt 221–530 | Not recorded | 24C10 Light Chain × 2 24C10 Heavy Chain × 2 | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;297.15 K;0.2 M HEPES: NaOH, pH 7.5, 8 % (w/v) PEG 8000, 8 % (v/v) Ethylene Glycol | Resolution 2.70 Å R-free 0.245 |
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.
1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | A0A1P8DD09_NORV |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A; PDBConstruct 2–311; UniProt 221–530 Author chain B; PDBConstruct 2–311; UniProt 221–530 |