Structure of PDB 1v1j Chain B

Receptor sequence
>1v1jB (length=150) Species: 1902 (Streptomyces coelicolor) [Search protein sequence]
PRSLANAPIMILNGPNLNLLGQRQPEIYGSDTLADVEALCVKAAAAHGGT
VDFRQSNHEGELVDWIHEARLNHCGIVINPAAYSHTSVAILDALNTCDGL
PVVEVHISNIHQREPFRHHSYVSQRADGVVAGCGVQGYVFGVERIAALAG
3D structure
PDB1v1j (1R,4S,5R)-3-Fluoro-1,4,5-Trihydroxy-2-Cyclohexene-1-Carboxylic Acid: The Fluoro Analogue of the Enolate Intermediate in the Reaction Catalyzed by Type II Dehydroquinases
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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) P15 N16 R23 Y28 N79 A82 E104 H106 R113
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 FA3 B Y28 N79 A81 A82 H85 H106 I107 S108 R117 Y28 N79 A81 A82 H85 H106 I107 S108 R117 MOAD: Ki=15uM
PDBbind-CN: -logKd/Ki=4.82,Ki=15uM
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:1v1j, PDBe:1v1j, PDBj:1v1j
PDBsum1v1j
PubMed15162210
UniProtP15474|AROQ_STRCO 3-dehydroquinate dehydratase (Gene Name=aroQ)

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