Structure of PDB 2c57 Chain A

Receptor sequence
>2c57A (length=164) Species: 210 (Helicobacter pylori) [Search protein sequence]
GSSHHHHHHSSSHMKILVIQGPNLNMLGGMVTLDQIHEIMQTFVKQGNLD
VELEFFQTNFEGEIIDKIQESVGSDYEGIIINPGAFSHTSIAIADAIMLA
GKPVIEVHLTNIQAREEFRKNSYTGAACGGVIMGFGPLGYNMALMAMVNI
LAEMKAFQEAQKNN
3D structure
PDB2c57 Crystal Structures of Helicobacter Pylori Type II Dehydroquinase Inhibitor Complexes: New Directions for Inhibitor Design.
ChainA
Resolution3.1 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 N76 A79 E100 H102 R109
Catalytic site (residue number reindexed from 1) P22 N23 N82 A85 E106 H108 R115
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 FA1 A N76 G78 A79 H82 H102 L103 T104 R113 N82 G84 A85 H88 H108 L109 T110 R119 PDBbind-CN: -logKd/Ki=3.43,Ki=370uM
BindingDB: Kd=370000nM
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:2c57, PDBe:2c57, PDBj:2c57
PDBsum2c57
PubMed16480265
UniProtQ48255|AROQ_HELPY 3-dehydroquinate dehydratase (Gene Name=aroQ)

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