Structure of PDB 1h0r Chain A Binding Site BS01

Receptor Information
>1h0r Chain A (length=139) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ELIVNVINGPNLGRLGRVYGGTTHDELVALIEREAAELGLKAVVRQSDSE
AQLLDWIHQAADAAEPVILNAGGLTHTSVALRDACAELSAPLIEVHISNV
HAREEFRRHSYLSPIATGVIVGLGIQGYLLALRYLAEHV
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 chain1h0r Chain A Residue 200 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1h0r The Two Types of 3-Dehydroquinase Have Distinct Structures But Catalyse the Same Overall Reaction
Resolution2.1 Å
Binding residue
(original residue number in PDB)		Y24 N75 G77 G78 H81 H101 I102 S103 R112
Binding residue
(residue number reindexed from 1)		Y19 N70 G72 G73 H76 H96 I97 S98 R107
Annotation score1
Binding affinityMOAD: Ki=200uM
PDBbind-CN: -logKd/Ki=3.70,Ki=200uM
BindingDB: Kd=200000nM,Ki=200000nM
Enzymatic activity
Catalytic site (original residue number in PDB) P11 N12 Y24 N75 G78 E99 H101 R108
Catalytic site (residue number reindexed from 1) P10 N11 Y19 N70 G73 E94 H96 R103
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
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1h0r, PDBe:1h0r, PDBj:1h0r
PDBsum1h0r
PubMed
UniProtP9WPX7|AROQ_MYCTU 3-dehydroquinate dehydratase (Gene Name=aroQ)

[Back to BioLiP]