Large T antigen
Simian virus 40
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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count | Chain A; UniProt 260–627 Chain B; UniProt 260–627 Chain C; UniProt 260–627 Chain D; UniProt 260–627 Chain E; UniProt 260–627 Chain F; UniProt 260–627 | Fragment:Helicase Domain, residues 260-627 | Cellular tumor antigen p53 × 6 (Q9NP68) ZN ZINC ION × 12 | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;298 K;5.4% PEG 4000, 73mM Mops Buffer, 22mM Lithium Sulfate, pH 6.5, VAPOR DIFFUSION, temperature 298K | Resolution 3.16 Å R-free 0.308 |
| 2 | Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count | Chain G; UniProt 260–627 Chain H; UniProt 260–627 Chain I; UniProt 260–627 Chain J; UniProt 260–627 Chain K; UniProt 260–627 Chain L; UniProt 260–627 | Fragment:Helicase Domain, residues 260-627 | Cellular tumor antigen p53 × 6 (Q9NP68) ZN ZINC ION × 12 | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;298 K;5.4% PEG 4000, 73mM Mops Buffer, 22mM Lithium Sulfate, pH 6.5, VAPOR DIFFUSION, temperature 298K | Resolution 3.16 Å R-free 0.308 |
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.
2 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | Q9DH70_SV40 |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A; PDBConstruct 3–370; UniProt 260–627 Author chain B; PDBConstruct 3–370; UniProt 260–627 Author chain C; PDBConstruct 3–370; UniProt 260–627 Author chain D; PDBConstruct 3–370; UniProt 260–627 Author chain E; PDBConstruct 3–370; UniProt 260–627 Author chain F; PDBConstruct 3–370; UniProt 260–627 Author chain G; PDBConstruct 3–370; UniProt 260–627 Author chain H; PDBConstruct 3–370; UniProt 260–627 Author chain I; PDBConstruct 3–370; UniProt 260–627 Author chain J; PDBConstruct 3–370; UniProt 260–627 Author chain K; PDBConstruct 3–370; UniProt 260–627 Author chain L; PDBConstruct 3–370; UniProt 260–627 |