Structure of PDB 1f93 Chain B Binding Site BS01
Receptor Information
>1f93 Chain B (length=99) Species:
10116
(Rattus norvegicus) [
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AHRLSAEERDQLLPNLRAVGWNELEGRDAIFKQFHFKDFNRAFGFMTRVA
LQAEKLDHHPEWFNVYNKVHITLSTHECAGLSERDINLASFIEQVAVSM
Ligand information
>1f93 Chain F (length=27) Species:
10090
(Mus musculus) [
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LSQLQTELLAALLESGLSKEALIQALG
Receptor-Ligand Complex Structure
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PDB
1f93
Structural basis of dimerization, coactivator recognition and MODY3 mutations in HNF-1alpha.
Resolution
2.6 Å
Binding residue
(original residue number in PDB)
A54 L55 E58
Binding residue
(residue number reindexed from 1)
A50 L51 E54
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.
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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Biological Process
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Cellular Component
External links
PDB
RCSB:1f93
,
PDBe:1f93
,
PDBj:1f93
PDBsum
1f93
PubMed
10966642
UniProt
P61459
|PHS_RAT Pterin-4-alpha-carbinolamine dehydratase (Gene Name=Pcbd1)
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