Structure of PDB 5ydb Chain A

Receptor sequence
>5ydbA (length=145) Species: 400667 (Acinetobacter baumannii ATCC 17978) [Search protein sequence]
STILVIHGPNLNLLGKREPEVYGHLTLDNINRQLIAQAEQASITLDTFQS
NWEGAIVDRIHQAQTEGVKLIIINPAALTHTSVALRDALLGVAIPFIEVH
LSNVHAREAFRHHSYLSDKAIGVICGLGAKGYSFALDYAIEKIQP
3D structure
PDB5ydb Crystal structure of the complex of type II dehydroquinate dehydratase from Acinetobacter baumannii with dehydroquinic acid at 1.76 Angstrom resolution
ChainA
Resolution1.76 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 R19 Y24 N76 A79 E100 H102 R109
Catalytic site (residue number reindexed from 1) P9 N10 R17 Y22 N74 A77 E98 H100 R107
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 DQA A N76 A78 A79 H82 H102 L103 S104 R113 N74 A76 A77 H80 H100 L101 S102 R111
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:5ydb, PDBe:5ydb, PDBj:5ydb
PDBsum5ydb
PubMed
UniProtA3M692|AROQ_ACIBT 3-dehydroquinate dehydratase (Gene Name=aroQ)

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