Structure of PDB 1qfe Chain B

Receptor sequence
>1qfeB (length=252) [Search protein sequence]
MKTVTVKNLIIGEGMPKIIVSLMGRDINSVKAEALAYREATFDILEWRVD
HFMDIASTQSVLTAARVIRDAMPDIPLLFTFRSAKEGGEQTITTQHYLTL
NRAAIDSGLVDMIDLELFTGDADVKATVDYAHAHNVYVVMSNHDFHQTPS
AEEMVSRLRKMQALGADIPKIAVMPQSKHDVLTLLTATLEMQQHYADRPV
ITMSMAKEGVISRLAGEVFGSAATFGAVKQASAPGQIAVNDLRSVLMILH
NA
3D structure
PDB1qfe The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction.
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E86 H143 K170
Catalytic site (residue number reindexed from 1) E86 H143 K170
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 DHS B E46 R48 R82 H143 K170 R213 F225 S232 A233 Q236 E46 R48 R82 H143 K170 R213 F225 S232 A233 Q236
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:0046279 3,4-dihydroxybenzoate biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1qfe, PDBe:1qfe, PDBj:1qfe
PDBsum1qfe
PubMed10360352
UniProtP24670|AROD_SALTI 3-dehydroquinate dehydratase (Gene Name=aroD)

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