Structure of PDB 2glp Chain D

Receptor sequence
>2glpD (length=152) Species: 102617 (Helicobacter pylori SS1) [Search protein sequence]
LQSQFFIEHILQILPHRYPMLLVDRITELQANQKIVAYKNITFNEDVFNG
HFPNKPIFPGVLIVEGMAQSGGFLAFTSLWGFDPEIAKTKIVYFMTIDKV
KFRIPVTPGDRLEYHLEVLKHKGMIWQVGGTAQVDGKVVAEAELKAMIAE
RE
3D structure
PDB2glp Structural basis for catalytic and inhibitory mechanisms of beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ).
ChainD
Resolution2.42 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) H51 I57 G60 V61 E65
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 BDE D F59 I64 F52 I57 PDBbind-CN: -logKd/Ki=5.01,Ki=9.7uM
BindingDB: IC50=39800nM
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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Cellular Component
External links
PDB RCSB:2glp, PDBe:2glp, PDBj:2glp
PDBsum2glp
PubMed18093984
UniProtO25928|FABZ_HELPY 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ (Gene Name=fabZ)

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