Function and Biology Details
Reaction catalysed:
4a-hydroxytetrahydrobiopterin = 6,7-dihydrobiopterin + H(2)O
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
homo tetramer (preferred)
Assembly name:
Pterin-4-alpha-carbinolamine dehydratase 2 (preferred)
PDBe Complex ID:
PDB-CPX-190028 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pterin-4-alpha-carbinolamine dehydratase 2
Molecule details ›
Chains: A, B
Length: 105 amino acids
Theoretical weight: 11.9 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Pterin 4 alpha carbinolamine dehydratase
Structure domains: Transcriptional coactivator/pterin dehydratase
Length: 105 amino acids
Theoretical weight: 11.9 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q9CZL5 (Residues: 33-136; Coverage: 77%)
Sequence domains: Pterin 4 alpha carbinolamine dehydratase
Structure domains: Transcriptional coactivator/pterin dehydratase
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ALS BEAMLINE 5.0.2
Spacegroup:
P3121
Expression system: Escherichia coli BL21(DE3)
