Structure of PDB 1og0 Chain E

Receptor sequence
>1og0E (length=335) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
GAEEDVRILGYDPLASPALLQVQIPATPTSLETAKRGRREAIDIITGKDD
RVLVIVGPCSIHDLEAAQEYALRLKKLSDELKGDLSIIMRAYLGLINDPD
VNNTFNINKGLQSARQLFVNLTNIGLPIGSEMLDTISPQYLADLVSFGAI
GARTTESQLHRELASGLSFPVGFKNGTDGTLNVAVDACQAAAHSHHFMSV
TKHGVAAITTTKGNEHCFVILRGGKKGTNYDAKSVAEAKAQLPAGSNGLM
IDYSHGNSNKDFRNQPKVNDVVCEQIANGENAITGVMIESNINEGNQGIP
KYGVSITDACIGWETTEDVLRKLAAAVRQRREVNK
3D structure
PDB1og0 Evolution of Feedback-Inhibited Beta /Alpha Barrel Isoenzymes by Gene Duplication and a Single Mutation.
ChainE
Resolution2.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.5.1.54: 3-deoxy-7-phosphoheptulonate synthase.
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 MN E C76 H282 E316 D342 C59 H255 E289 D308
BS02 PHE E E21 D22 I25 E4 D5 I8
BS03 PHE E T162 P165 Q166 A169 L194 S195 T135 P138 Q139 A142 L167 S168
Gene Ontology
Molecular Function
GO:0003849 3-deoxy-7-phosphoheptulonate synthase activity
GO:0016740 transferase activity
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0009058 biosynthetic process
GO:0009073 aromatic amino acid family biosynthetic process
GO:0009423 chorismate biosynthetic process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:1og0, PDBe:1og0, PDBj:1og0
PDBsum1og0
PubMed
UniProtP32449|AROG_YEAST Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited (Gene Name=ARO4)

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