Structure of PDB 1h0r Chain A

Receptor sequence
>1h0rA (length=139) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
ELIVNVINGPNLGRLGRVYGGTTHDELVALIEREAAELGLKAVVRQSDSE
AQLLDWIHQAADAAEPVILNAGGLTHTSVALRDACAELSAPLIEVHISNV
HAREEFRRHSYLSPIATGVIVGLGIQGYLLALRYLAEHV
3D structure
PDB1h0r The Two Types of 3-Dehydroquinase Have Distinct Structures But Catalyse the Same Overall Reaction
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) 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.
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 Y24 N75 G77 G78 H81 H101 I102 S103 R112 Y19 N70 G72 G73 H76 H96 I97 S98 R107 MOAD: Ki=200uM
PDBbind-CN: -logKd/Ki=3.70,Ki=200uM
BindingDB: Kd=200000nM,Ki=200000nM
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

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External links
PDB RCSB:1h0r, PDBe:1h0r, PDBj:1h0r
PDBsum1h0r
PubMed
UniProtP9WPX7|AROQ_MYCTU 3-dehydroquinate dehydratase (Gene Name=aroQ)

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