BioLiP

Structure of PDB 1v1j Chain A

Receptor sequence

>1v1jA (length=150) Species: 1902 (Streptomyces coelicolor) [Search protein sequence]

PRSLANAPIMILNGPNLNLLGQRQPEIYGSDTLADVEALCVKAAAAHGGT
VDFRQSNHEGELVDWIHEARLNHCGIVINPAAYSHTSVAILDALNTCDGL
PVVEVHISNIHQREPFRHHSYVSQRADGVVAGCGVQGYVFGVERIAALAG

3D structure

PDB

1v1j (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

Chain

Resolution

2.2 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	A	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

PDB	RCSB:1v1j, PDBe:1v1j, PDBj:1v1j
PDBsum	1v1j
PubMed	15162210
UniProt	P15474\|AROQ_STRCO 3-dehydroquinate dehydratase (Gene Name=aroQ)