Function and Biology Details
Reaction catalysed:
The enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
C-terminal processing peptidase, chloroplastic (preferred)
PDBe Complex ID:
PDB-CPX-126431 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
C-terminal processing peptidase, chloroplastic
Molecule details ›
Chain: A
Length: 388 amino acids
Theoretical weight: 40.75 KDa
Source organism: Tetradesmus obliquus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 388 amino acids
Theoretical weight: 40.75 KDa
Source organism: Tetradesmus obliquus
Expression system: Escherichia coli
UniProt:
- Canonical:
O04073 (Residues: 78-464; Coverage: 83%)
Sequence domains:
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU RU200
Spacegroup:
C2
Expression system: Escherichia coli
