Structure of PDB 5hud Chain A Binding Site BS01
Receptor Information
>5hud Chain A (length=444) Species:
1718
(Corynebacterium glutamicum) [
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PEGMQQQFEDTISRDAKQQPTWDRAQAENVRKILESVPPIVVAPEVLELK
QKLADVANGKAFLLQGGDCAETFESNTEPHIRANVKTLLQMAVVLTYGAS
TPVIKMARIAGQYAKPRSSDLDGNGLPNYRGDIVNGVEATPEARRHDPAR
MIRAYANASAAMNLVRALTSSGTADLYRLSEWNREFVANSPAGARYEALA
REIDSGLRFMEACGVSDESLRAADIYCSHEALLVDYERSMLRLATDEEGN
EELYDLSAHQLWIGERTRGMDDFHVNFASMISNPIGIKIGPGITPEEAVA
YADKLDPNFEPGRLTIVARMGHDKVRSVLPGVIQAVEASGHKVIWQSDPM
HGNTFTASNGYKTRHFDKVIDEVQGFFEVHRALGTHPGGIHIEFTGEDVT
ECLGGAEDITDVDLPGRYESACDPRLNTQQSLELAFLVAEMLRN
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
5hud Chain A Residue 506 [
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Receptor-Ligand Complex Structure
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PDB
5hud
Inter-Enzyme Allosteric Regulation of Chorismate Mutase in Corynebacterium glutamicum: Structural Basis of Feedback Activation by Trp.
Resolution
2.15 Å
Binding residue
(original residue number in PDB)
C97 H379 E421 D451
Binding residue
(residue number reindexed from 1)
C69 H351 E393 D423
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:0046872
metal ion binding
Biological Process
GO:0008652
amino acid biosynthetic process
GO:0009073
aromatic amino acid family biosynthetic process
GO:0009423
chorismate biosynthetic process
View graph for
Molecular Function
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Biological Process
External links
PDB
RCSB:5hud
,
PDBe:5hud
,
PDBj:5hud
PDBsum
5hud
PubMed
29178787
UniProt
Q8NNL5
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