Structure of PDB 1dcp Chain F

Receptor sequence
>1dcpF (length=99) Species: 10116 (Rattus norvegicus) [Search protein sequence]
HRLSAEERDQLLPNLRAVGWNELEGRDAIFKQFHFKDFNRAFGFMTRVAL
QAEKLDHHPEWFNVYNKVHITLSTHECAGLSERDINLASFIEQVAVSMT
3D structure
PDB1dcp High-resolution structures of the bifunctional enzyme and transcriptional coactivator DCoH and its complex with a product analogue.
ChainF
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 F D61 H62 H63 S78 T79 H80 D56 H57 H58 S73 T74 H75
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

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Molecular Function

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Cellular Component
External links
PDB RCSB:1dcp, PDBe:1dcp, PDBj:1dcp
PDBsum1dcp
PubMed8897596
UniProtP61459|PHS_RAT Pterin-4-alpha-carbinolamine dehydratase (Gene Name=Pcbd1)

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