Structure of PDB 1gu1 Chain J

Receptor sequence
>1gu1J (length=149) Species: 1902 (Streptomyces coelicolor) [Search protein sequence]
RSLANAPIMILNGPNLNLLGQRQPEIYGSDTLADVEALCVKAAAAHGGTV
DFRQSNHEGELVDWIHEARLNHCGIVINPAAYSHTSVAILDALNTCDGLP
VVEVHISNIHQREPFRHHSYVSQRADGVVAGCGVQGYVFGVERIAALAG
3D structure
PDB1gu1 The Structure and Mechanism of the Type II Dehydroquinase from Streptomyces Coelicolor
ChainJ
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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) P14 N15 R22 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 FA1 J Y28 N79 A81 A82 H85 H106 I107 S108 R117 Y27 N78 A80 A81 H84 H105 I106 S107 R116 MOAD: Ki=30uM
BindingDB: Kd=30000nM
BS02 GOL J N16 L17 L20 Y28 N15 L16 L19 Y27
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1gu1, PDBe:1gu1, PDBj:1gu1
PDBsum1gu1
PubMed11937054
UniProtP15474|AROQ_STRCO 3-dehydroquinate dehydratase (Gene Name=aroQ)

[Back to BioLiP]