Structure of PDB 1gg1 Chain D Binding Site BS02
Receptor Information
>1gg1 Chain D (length=340) Species:
562
(Escherichia coli) [
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LRIKEIKELLPPVALLEKFPATENAANTVAHARKAIHKILKGNDDRLLVV
IGPCSIHDPVAAKEYATRLLALREELKDELEIVMRVYFEKPRTTVGWKGL
INDPHMDNSFQINDGLRIARKLLLDINDSGLPAAGEFLDMITPQYLADLM
SWGAIGARTTESQVHRELASGLSCPVGFKNGTDGTIKVAIDAINAAGAPH
CFLSVTKWGHSAIVNTSGNGDCHIILRGGKEPNYSAKHVAEVKEGLNKAG
LPAQVMIDFSHANSSKQFKKQMDVCADVCQQIAGGEKAIIGVMVESHLVE
GNQSLEPLAYGKSITDACIGWEDTDALLRQLANAVKARRG
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
1gg1 Chain D Residue 371 [
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Receptor-Ligand Complex Structure
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PDB
1gg1
Structure of 3-deoxy-d-arabino-heptulosonate-7-phosphate synthase from Escherichia coli: comparison of the Mn(2+)*2-phosphoglycolate and the Pb(2+)*2-phosphoenolpyruvate complexes and implications for catalysis.
Resolution
2.0 Å
Binding residue
(original residue number in PDB)
C61 H268 E302 D326
Binding residue
(residue number reindexed from 1)
C54 H261 E295 D316
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
GO:0042802
identical protein binding
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:0005737
cytoplasm
GO:0005829
cytosol
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1gg1
,
PDBe:1gg1
,
PDBj:1gg1
PDBsum
1gg1
PubMed
10926516
UniProt
P0AB91
|AROG_ECOLI Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive (Gene Name=aroG)
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