PROTEIN (FIBER KNOB PROTEIN)
Human adenovirus 12
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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count | Chain A; UniProt 403–587 Chain B; UniProt 403–587 Chain C; UniProt 403–587 | Fragment:KNOB | No other associated polymer | X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;26% PEG 3350, pH 7.0 | Resolution 2.60 Å R-free 0.290 |
| 2 | Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count | Chain D; UniProt 403–587 Chain E; UniProt 403–587 Chain F; UniProt 403–587 | Fragment:KNOB | No other associated polymer | X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;26% PEG 3350, pH 7.0 | Resolution 2.60 Å R-free 0.290 |
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.
3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | FIBP_ADE12 |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A; PDBConstruct 1–185; UniProt 403–587 Author chain B; PDBConstruct 1–185; UniProt 403–587 Author chain C; PDBConstruct 1–185; UniProt 403–587 Author chain D; PDBConstruct 1–185; UniProt 403–587 Author chain E; PDBConstruct 1–185; UniProt 403–587 Author chain F; PDBConstruct 1–185; UniProt 403–587 |