Structure of PDB 1og0 Chain C Binding Site BS01
Receptor Information
>1og0 Chain C (length=346) Species:
4932
(Saccharomyces cerevisiae) [
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GAEEDVRILGYDPLASPALLQVQIPATPTSLETAKRGRREAIDIITGKDD
RVLVIVGPCSIHDLEAAQEYALRLKKLSDELKGDLSIIMRAYLEKWKGLI
NDPDVNNTFNINKGLQSARQLFVNLTNIGLPIGSEMLDTISPQYLADLVS
FGAIGARTTESQLHRELASGLSFPVGFKNGTDGTLNVAVDACQAAAHSHH
FMSVTKHGVAAITTTKGNEHCFVILRGGKKGTNYDAKSVAEAKAQLPAGS
NGLMIDYSHGNSNKDFRNQPKVNDVVCEQIANGENAITGVMIESNINEGN
QGIPAEGKAGLKYGVSITDACIGWETTEDVLRKLAAAVRQRREVNK
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
1og0 Chain C Residue 400 [
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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)
C76 H282 E316 D342
Binding residue
(residue number reindexed from 1)
C59 H259 E293 D319
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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