Caspase recruitment domain-containing protein 8
Homo sapiens
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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count | Chain A; UniProt 345–431 Chain B; UniProt 345–431 Chain C; UniProt 345–431 Chain D; UniProt 345–431 Chain E; UniProt 345–431 Chain F; UniProt 345–431 Chain G; UniProt 345–431 Chain H; UniProt 345–431 Chain I; UniProt 345–431 Chain J; UniProt 345–431 Chain K; UniProt 345–431 Chain L; UniProt 345–431 | Not recorded | No other associated polymer | ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE | Resolution 3.70 Å R-free 0.302 |
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.
4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | CARD8_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A; PDBConstruct 5–91; UniProt 345–431 Author chain B; PDBConstruct 5–91; UniProt 345–431 Author chain C; PDBConstruct 5–91; UniProt 345–431 Author chain D; PDBConstruct 5–91; UniProt 345–431 Author chain E; PDBConstruct 5–91; UniProt 345–431 Author chain F; PDBConstruct 5–91; UniProt 345–431 Author chain G; PDBConstruct 5–91; UniProt 345–431 Author chain H; PDBConstruct 5–91; UniProt 345–431 Author chain I; PDBConstruct 5–91; UniProt 345–431 Author chain J; PDBConstruct 5–91; UniProt 345–431 Author chain K; PDBConstruct 5–91; UniProt 345–431 Author chain L; PDBConstruct 5–91; UniProt 345–431 |