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:
- not assigned
Biological process:
Cellular component:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-180765 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Small vasohibin-binding protein
Molecule details ›
Chain: A
Length: 46 amino acids
Theoretical weight: 5.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
Sequence domains: Coiled-coil domain-containing protein 23
Length: 46 amino acids
Theoretical weight: 5.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
- Canonical:
Q8N300 (Residues: 3-48; Coverage: 70%)
Sequence domains: Coiled-coil domain-containing protein 23
Tubulinyl-Tyr carboxypeptidase 1
Detyrosinated tubulin alpha-1A chain
Molecule details ›
Chain: C
Length: 8 amino acids
Theoretical weight: 915 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Length: 8 amino acids
Theoretical weight: 915 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
- Canonical: Q71U36 (Residues: 444-451; Coverage: 2%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SSRF BEAMLINE BL17U1
Spacegroup:
P21212
Expression systems:
- Escherichia coli 'BL21-Gold(DE3)pLysS AG'
- Escherichia coli
- Not provided
