Structure of PDB 1gu1 Chain B Binding Site BS01

Receptor Information
>1gu1 Chain B (length=149) Species: 1902 (Streptomyces coelicolor) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RSLANAPIMILNGPNLNLLGQRQPEIYGSDTLADVEALCVKAAAAHGGTV
DFRQSNHEGELVDWIHEARLNHCGIVINPAAYSHTSVAILDALNTCDGLP
VVEVHISNIHQREPFRHHSYVSQRADGVVAGCGVQGYVFGVERIAALAG
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 chain1gu1 Chain B Residue 201 [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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PDB1gu1 The Structure and Mechanism of the Type II Dehydroquinase from Streptomyces Coelicolor
Resolution1.8 Å
Binding residue
(original residue number in PDB)		Y28 N79 A81 A82 H85 H106 I107 S108 R117
Binding residue
(residue number reindexed from 1)		Y27 N78 A80 A81 H84 H105 I106 S107 R116
Annotation score1
Binding affinityMOAD: Ki=30uM
PDBbind-CN: -logKd/Ki=4.52,Ki=30uM
BindingDB: Kd=30000nM
Enzymatic activity
Catalytic site (original residue number in PDB) P15 N16 R23 Y28 N79 A82 E104 H106 R113
Catalytic site (residue number reindexed from 1) P14 N15 R22 Y27 N78 A81 E103 H105 R112
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1gu1, PDBe:1gu1, PDBj:1gu1
PDBsum1gu1
PubMed11937054
UniProtP15474|AROQ_STRCO 3-dehydroquinate dehydratase (Gene Name=aroQ)

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