Structure of PDB 2c57 Chain A Binding Site BS01

Receptor Information
>2c57 Chain A (length=164) Species: 210 (Helicobacter pylori) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GSSHHHHHHSSSHMKILVIQGPNLNMLGGMVTLDQIHEIMQTFVKQGNLD
VELEFFQTNFEGEIIDKIQESVGSDYEGIIINPGAFSHTSIAIADAIMLA
GKPVIEVHLTNIQAREEFRKNSYTGAACGGVIMGFGPLGYNMALMAMVNI
LAEMKAFQEAQKNN
Ligand information
Ligand IDFA1
InChIInChI=1S/C7H10O5/c8-4-1-2-7(12,6(10)11)3-5(4)9/h1-2,4-5,8-9,12H,3H2,(H,10,11)/t4-,5-,7+/m1/s1
InChIKeyVTEDVYGIJPLVFF-XAHCXIQSSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C1C(C(C=CC1(C(=O)O)O)O)O
OpenEye OEToolkits 1.5.0C1[C@H]([C@@H](C=C[C@]1(C(=O)O)O)O)O
CACTVS 3.341O[C@@H]1C[C@@](O)(C=C[C@H]1O)C(O)=O
ACDLabs 10.04O=C(O)C1(O)C=CC(O)C(O)C1
CACTVS 3.341O[CH]1C[C](O)(C=C[CH]1O)C(O)=O
FormulaC7 H10 O5
Name2,3 -ANHYDRO-QUINIC ACID
ChEMBLCHEMBL190265
DrugBankDB02801
ZINC
PDB chain2c57 Chain A Residue 1159 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2c57 Crystal Structures of Helicobacter Pylori Type II Dehydroquinase Inhibitor Complexes: New Directions for Inhibitor Design.
Resolution3.1 Å
Binding residue
(original residue number in PDB)		N76 G78 A79 H82 H102 L103 T104 R113
Binding residue
(residue number reindexed from 1)		N82 G84 A85 H88 H108 L109 T110 R119
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=3.43,Ki=370uM
BindingDB: Kd=370000nM
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.
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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