Structure of PDB 3dp2 Chain B

Receptor sequence
>3dp2B (length=150) Species: 210 (Helicobacter pylori) [Search protein sequence]
SQFFIEHILQILPHRYPMLLVDRITELQANQKIVAYKNITFNEDVFNGHF
PNKPIFPGVLIVEGMAQSGGFLAFTSLWGFDPEIAKTKIVYFMTIDKVKF
RIPVTPGDRLEYHLEVLKHKGMIWQVGGTAQVDGKVVAEAELKAMIAERE
3D structure
PDB3dp2 Discovering potent inhibitors against the beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ) of Helicobacter pylori: structure-based design, synthesis, bioassay, and crystal structure determination.
ChainB
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H58 I64 G67 V68 E72
Catalytic site (residue number reindexed from 1) H49 I55 G58 V59 E63
Enzyme Commision number 4.2.1.59: 3-hydroxyacyl-[acyl-carrier-protein] 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 4BE B I98 Y100 R158 E159 I89 Y91 R149 E150 MOAD: ic50=1.5uM
PDBbind-CN: -logKd/Ki=5.82,IC50=1.50uM
Gene Ontology
Molecular Function
GO:0016829 lyase activity
GO:0016836 hydro-lyase activity
GO:0019171 (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0009245 lipid A biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3dp2, PDBe:3dp2, PDBj:3dp2
PDBsum3dp2
PubMed19309082
UniProtQ5G940

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