Structure of PDB 1dcp Chain C

Receptor sequence

>1dcpC (length=99) Species: 10116 (Rattus norvegicus)

HRLSAEERDQLLPNLRAVGWNELEGRDAIFKQFHFKDFNRAFGFMTRVAL
QAEKLDHHPEWFNVYNKVHITLSTHECAGLSERDINLASFIEQVAVSMT

3D structure

• PDB: 1dcp High-resolution structures of the bifunctional enzyme and transcriptional coactivator DCoH and its complex with a product analogue.
• Chain: C
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E58 H62 H63 H80 E81 D89
• Catalytic site (residue number reindexed from 1): E53 H57 H58 H75 E76 D84
• Enzyme Commision number: 4.2.1.96: 4a-hydroxytetrahydrobiopterin dehydratase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	HBI	C	D61 H62 H63	D56 H57 H58

Gene Ontology

Molecular Function

• GO:0003713 transcription coactivator activity
• GO:0004505 phenylalanine 4-monooxygenase activity
• GO:0008124 4-alpha-hydroxytetrahydrobiopterin dehydratase activity
• GO:0016829 lyase activity
• GO:0042802 identical protein binding

Biological Process

• GO:0006558 L-phenylalanine metabolic process
• GO:0006729 tetrahydrobiopterin biosynthetic process
• GO:0008150 biological_process
• GO:0019293 tyrosine biosynthetic process, by oxidation of phenylalanine
• GO:0043393 regulation of protein binding
• GO:0045893 positive regulation of DNA-templated transcription

Cellular Component

• GO:0005634 nucleus
• GO:0005737 cytoplasm

External links

• PDB: RCSB:1dcp, PDBe:1dcp, PDBj:1dcp
• PDBsum: 1dcp
• PubMed: 8897596
• UniProt: P61459|PHS_RAT Pterin-4-alpha-carbinolamine dehydratase (Gene Name=Pcbd1)