6ocf

X-ray diffraction
2.1Å resolution

The crystal structure of VASH1-SVBP complex

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis of tubulin detyrosination by vasohibins.
Nat. Struct. Mol. Biol. (2019)
PMID: 31235910

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:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tubulinyl-Tyr carboxypeptidase 1 Chain: A
Molecule details ›
Chain: A
Length: 248 amino acids
Theoretical weight: 29.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q7L8A9 (Residues: 58-305; Coverage: 68%)
Gene names: KIAA1036, VASH, VASH1
Sequence domains: Vasohibin
Small vasohibin-binding protein Chain: B
Molecule details ›
Chain: B
Length: 49 amino acids
Theoretical weight: 6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8N300 (Residues: 18-66; Coverage: 74%)
Gene names: CCDC23, SVBP

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I4122
Unit cell:
a: 100.558Å b: 100.558Å c: 206.73Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.196 0.222
Expression system: Escherichia coli BL21