Mitochondrial chaperone BCS1
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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count | Chain A; UniProt 1–456 Chain B; UniProt 1–456 Chain C; UniProt 1–456 Chain D; UniProt 1–456 Chain E; UniProt 1–456 Chain F; UniProt 1–456 Chain G; UniProt 1–456 | Not recorded | No other associated polymer | ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE | Resolution 4.40 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.
5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | BCS1_YEAST |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A; PDBConstruct 1–456; UniProt 1–456 Author chain B; PDBConstruct 1–456; UniProt 1–456 Author chain C; PDBConstruct 1–456; UniProt 1–456 Author chain D; PDBConstruct 1–456; UniProt 1–456 Author chain E; PDBConstruct 1–456; UniProt 1–456 Author chain F; PDBConstruct 1–456; UniProt 1–456 Author chain G; PDBConstruct 1–456; UniProt 1–456 |