Structure of PDB 1f93 Chain D

Receptor sequence
>1f93D (length=100) Species: 10116 (Rattus norvegicus) [Search protein sequence]
AHRLSAEERDQLLPNLRAVGWNELEGRDAIFKQFHFKDFNRAFGFMTRVA
LQAEKLDHHPEWFNVYNKVHITLSTHECAGLSERDINLASFIEQVAVSMT
3D structure
PDB1f93 Structural basis of dimerization, coactivator recognition and MODY3 mutations in HNF-1alpha.
ChainD
Resolution2.6 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) E54 H58 H59 H76 E77 D85
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 peptide D N44 R45 G48 T51 R52 L55 N40 R41 G44 T47 R48 L51
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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Cellular Component
External links
PDB RCSB:1f93, PDBe:1f93, PDBj:1f93
PDBsum1f93
PubMed10966642
UniProtP61459|PHS_RAT Pterin-4-alpha-carbinolamine dehydratase (Gene Name=Pcbd1)

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