Structure of PDB 2c57 Chain E

Receptor sequence
>2c57E (length=153) Species: 210 (Helicobacter pylori) [Search protein sequence]
MKILVIQGPNLNMLGHRGMVTLDQIHEIMQTFVKQGNLDVELEFFQTNFE
GEIIDKIQESVGSDYEGIIINPGAFSHTSIAIADAIMLAGKPVIEVHLTN
IQAREEFRKNSYTGAACGGVIMGFGPLGYNMALMAMVNILAEMKAFQEAQ
KNN
3D structure
PDB2c57 Crystal Structures of Helicobacter Pylori Type II Dehydroquinase Inhibitor Complexes: New Directions for Inhibitor Design.
ChainE
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 R17 N76 A79 E100 H102 R109
Catalytic site (residue number reindexed from 1) P9 N10 R17 N71 A74 E95 H97 R104
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 E N76 G78 A79 H82 H102 L103 T104 R113 N71 G73 A74 H77 H97 L98 T99 R108 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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