Function and Biology Details
Reaction catalysed:
Cleavage of the -Glu-|-Tyr bond to release the C-terminal tyrosine residue from the native tyrosinated tubulin. Inactive on Z-Glu-Tyr.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181638 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Small vasohibin-binding protein
Molecule details ›
Chains: A, C
Length: 66 amino acids
Theoretical weight: 7.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
Sequence domains: Coiled-coil domain-containing protein 23
Length: 66 amino acids
Theoretical weight: 7.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
- Canonical:
Q8N300 (Residues: 1-66; Coverage: 100%)
Sequence domains: Coiled-coil domain-containing protein 23
Tubulinyl-Tyr carboxypeptidase 1
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SSRF BEAMLINE BL18U1
Spacegroup:
P212121
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
