Structure of PDB 2wks Chain D

Receptor sequence
>2wksD (length=153) Species: 210 (Helicobacter pylori) [Search protein sequence]
MKILVIQGPNLNMLGHRDPRLYGMVTLDQIHEIMQTFVKQGNLDVELEFF
QTNFEGEIIDKIQESVGSDYEGIIINPGAFSHTSIAIADAIMLAGKPVIE
VHLTNIQAREEFRKNSYTGAACGGVIMGFGPLGYNMALMAMVNILAEMKA
FQE
3D structure
PDB2wks Synthesis and biological evaluation of new nanomolar competitive inhibitors of Helicobacter pylori type II dehydroquinase. Structural details of the role of the aromatic moieties with essential residues.
ChainD
Resolution2.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) P9 N10 R17 Y22 N76 A79 E100 H102 R109
Catalytic site (residue number reindexed from 1) P9 N10 R17 Y22 N76 A79 E100 H102 R109
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 CB6 D N10 L11 Y22 N76 G78 A79 H102 L103 T104 R113 N10 L11 Y22 N76 G78 A79 H102 L103 T104 R113
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:0019631 quinate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2wks, PDBe:2wks, PDBj:2wks
PDBsum2wks
PubMed19911771
UniProtQ48255|AROQ_HELPY 3-dehydroquinate dehydratase (Gene Name=aroQ)

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