Structure of PDB 1og0 Chain B Binding Site BS02

Receptor Information
>1og0 Chain B (length=346) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AEEDVRILGYDPLASPALLQVQIPATPTSLETAKRGRREAIDIITGKDDR
VLVIVGPCSIHDLEAAQEYALRLKKLSDELKGDLSIIMRAYLEKPVGWKG
LINDPDVNNTFNINKGLQSARQLFVNLTNIGLPIGSEMLDTISPQYLADL
VSFGAIGARTTESQLHRELASGLSFPVGFKNGTDGTLNVAVDACQAAAHS
HHFMSVTKHGVAAITTTKGNEHCFVILRGGKGTNYDAKSVAEAKAQLPAG
SNGLMIDYSHGNSNKDFRNQPKVNDVVCEQIANGENAITGVMIESNINEG
NQGIPAEGKALKYGVSITDACIGWETTEDVLRKLAAAVRQRREVNK
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain1og0 Chain B Residue 400 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1og0 Evolution of Feedback-Inhibited Beta /Alpha Barrel Isoenzymes by Gene Duplication and a Single Mutation.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		C76 H282 E316 D342
Binding residue
(residue number reindexed from 1)		C58 H260 E294 D319
Annotation score1
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
PDBsum1og0
PubMed
UniProtP32449|AROG_YEAST Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited (Gene Name=ARO4)

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