Structure of PDB 4iuo Chain B

Receptor sequence
>4iuoB (length=260) Species: 99287 (Salmonella enterica subsp. enterica serovar Typhimurium str. LT2) [Search protein sequence]
NLYFQSNAMKTVTVRDLVVGEGAPKIIVSLMGKTITDVKSEALAYREADF
DILEWRVDHFANVTTAESVLEAAGAIREIITDKPLLFTFRSAKEGGEQAL
TTGQYIDLNRAAVDSGLVDMIDLELFTGDDEVKATVGYAHQHNVAVIMSN
HDFHKTPAAEEIVQRLRKMQELGADIPMIAVMPQTKADVLTLLTATVEMQ
ERYADRPIITMSMSKTGVISRLAGEVFGSAATFGAVKKASAPGQISVADL
RTVLTILHQA
3D structure
PDB4iuo Crystal structures of type I dehydroquinate dehydratase in complex with quinate and shikimate suggest a novel mechanism of schiff base formation.
ChainB
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E86 H143 M170
Catalytic site (residue number reindexed from 1) E94 H151 M178
Enzyme Commision number 4.2.1.10: 3-dehydroquinate dehydratase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 QIC B E46 R48 R82 H143 R213 F225 S232 A233 Q236 E54 R56 R90 H151 R221 F233 S240 A241 Q244
Gene Ontology
Molecular Function
GO:0003855 3-dehydroquinate dehydratase activity
GO:0016829 lyase activity
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0009073 aromatic amino acid family biosynthetic process
GO:0009423 chorismate biosynthetic process
GO:0046279 3,4-dihydroxybenzoate biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4iuo, PDBe:4iuo, PDBj:4iuo
PDBsum4iuo
PubMed24437575
UniProtP58687|AROD_SALTY 3-dehydroquinate dehydratase (Gene Name=aroD)

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