Structure of PDB 1gtz Chain C

Receptor sequence
>1gtzC (length=149) Species: 1902 (Streptomyces coelicolor) [Search protein sequence]
RSLANAPIMILNGPNLNLLGQAQPEIYGSDTLADVEALCVKAAAAHGGTV
DFRQSNHEGELVDWIHEARLNHCGIVINPAAYSHTSVAILDALNTCDGLP
VVEVHISNIHQREPFRHHSYVSQRADGVVAGCGVQGYVFGVERIAALAG
3D structure
PDB1gtz The Structure and Mechanism of the Type II Dehydroquinase from Streptomyces Coelicolor
ChainC
Resolution1.6 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 A23 Y28 N79 A82 E104 H106 R113
Catalytic site (residue number reindexed from 1) P14 N15 A22 Y27 N78 A81 E103 H105 R112
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 DHK C Y28 A81 A82 H85 I107 S108 R117 Y27 A80 A81 H84 I106 S107 R116
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:1gtz, PDBe:1gtz, PDBj:1gtz
PDBsum1gtz
PubMed11937054
UniProtP15474|AROQ_STRCO 3-dehydroquinate dehydratase (Gene Name=aroQ)

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