› 1dcp

X-ray diffraction
2.3Å resolution

DCOH, A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR, COMPLEXED WITH BIOPTERIN

Released:
DOI: 10.2210/pdb1dcp/pdb
PDB entry 1dcp coloured by chain, front view.
PDB entry 1dcp coloured by chain, side view.
PDB entry 1dcp coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
High-resolution structures of the bifunctional enzyme and transcriptional coactivator DCoH and its complex with a product analogue.
Cronk JD, Endrizzi JA, Alber T
Protein Sci 5 1963-72 (1996)
PMID: 8897596

Function and Biology Details

Reaction catalysed: 
4a-hydroxytetrahydrobiopterin = 6,7-dihydrobiopterin + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158261 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pterin-4-alpha-carbinolamine dehydratase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 104 amino acids
Theoretical weight: 12.02 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P61459 (Residues: 1-104; Coverage: 100%)
Gene names: Dcoh, Pcbd, Pcbd1
Sequence domains: Pterin 4 alpha carbinolamine dehydratase
Structure domains: Transcriptional coactivator/pterin dehydratase

Ligands and Environments

1 bound ligand:
Ligand HBI 8 x HBI
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 105.7Å b: 105.7Å c: 196.17Å
α: 90° β: 90° γ: 120°
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Tetrahydrobiopterin biosynthesis, regeneration and functions.
Thöny et al. (2000)
2 more

5 mentions without citation

Structural space of protein-protein interfaces is degenerate, close to complete, and highly connected.
Gao et al. (2010)
4 more