Structure of PDB 4b6r Chain C

Receptor sequence
>4b6rC (length=157) Species: 85962 (Helicobacter pylori 26695) [Search protein sequence]
MKILVIQGPNLNMLGHRDPRLYGMVTLDQIHEIMQTFVKQGNLDVELEFF
QTNFEGEIIDKIQESVGSDYEGIIINPGAFSHTSIAIADAIMLAGKPVIE
VHLTNIQAREEFRKNSYTGAACGGVIMGFGPLGYNMALMAMVNILAEMKA
FQEAQKN
3D structure
PDB4b6r Mechanistic basis of the inhibition of type II dehydroquinase by (2S)- and (2R)-2-benzyl-3-dehydroquinic acids.
ChainC
Resolution2.0 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 3DQ C D89 L93 D89 L93 MOAD: Ki=1420nM
PDBbind-CN: -logKd/Ki=5.85,Ki=1420nM
BS02 3DQ C Y22 N76 G78 A79 H82 H102 L103 T104 R113 Y22 N76 G78 A79 H82 H102 L103 T104 R113 MOAD: Ki=1420nM
PDBbind-CN: -logKd/Ki=5.85,Ki=1420nM
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:4b6r, PDBe:4b6r, PDBj:4b6r
PDBsum4b6r
PubMed23198883
UniProtQ48255|AROQ_HELPY 3-dehydroquinate dehydratase (Gene Name=aroQ)

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