Structure of PDB 1og0 Chain G Binding Site BS03
Receptor Information
>1og0 Chain G (length=342) Species:
4932
(Saccharomyces cerevisiae) [
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AEEDVRILGYDPLASPALLQVQIPATPTSLETAKRGRREAIDIITGKDDR
VLVIVGPCSIHDLEAAQEYALRLKKLSDELKGDLSIIMRAYLEKPWKGLI
NDPDVNNTFNINKGLQSARQLFVNLTNIGLPIGSEMLDTISPQYLADLVS
FGAIGARTTESQLHRELASGLSFPVGFKNGTDGTLNVAVDACQAAAHSHH
FMSVTKHGVAAITTTKGNEHCFVILRGGKKGTNYDAKSVAEAKAQLPAGS
NGLMIDYSHGNSNKDFRNQPKVNDVVCEQIANGENAITGVMIESNINEGN
QIPAEAGLKYGVSITDACIGWETTEDVLRKLAAAVRQRREVN
Ligand information
Ligand ID
PHE
InChI
InChI=1S/C9H11NO2/c10-8(9(11)12)6-7-4-2-1-3-5-7/h1-5,8H,6,10H2,(H,11,12)/t8-/m0/s1
InChIKey
COLNVLDHVKWLRT-QMMMGPOBSA-N
SMILES
Software
SMILES
CACTVS 3.341
N[CH](Cc1ccccc1)C(O)=O
CACTVS 3.341
N[C@@H](Cc1ccccc1)C(O)=O
OpenEye OEToolkits 1.5.0
c1ccc(cc1)CC(C(=O)O)N
OpenEye OEToolkits 1.5.0
c1ccc(cc1)C[C@@H](C(=O)O)N
ACDLabs 10.04
O=C(O)C(N)Cc1ccccc1
Formula
C9 H11 N O2
Name
PHENYLALANINE
ChEMBL
CHEMBL301523
DrugBank
DB00120
ZINC
ZINC000000105196
PDB chain
1og0 Chain H Residue 1012 [
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Receptor-Ligand Complex Structure
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PDB
1og0
Evolution of Feedback-Inhibited Beta /Alpha Barrel Isoenzymes by Gene Duplication and a Single Mutation.
Resolution
2.7 Å
Binding residue
(original residue number in PDB)
E21 D22 Y28
Binding residue
(residue number reindexed from 1)
E3 D4 Y10
Annotation score
1
Enzymatic activity
Enzyme Commision number
2.5.1.54
: 3-deoxy-7-phosphoheptulonate synthase.
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1og0
,
PDBe:1og0
,
PDBj:1og0
PDBsum
1og0
PubMed
UniProt
P32449
|AROG_YEAST Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited (Gene Name=ARO4)
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