Structure of PDB 5t9c Chain E

Receptor sequence
>5t9cE (length=263) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
NLLSPDRILTVAHRGASGYVPEHTILSYETAQKMKADFIELDLQMTKDGK
LIVMHDEKLDRTTNGMGWVKDHTLADIKKLDAGSWFNEAYPEKAKPQYVG
LKVPTLEEVLDRFGKHANYYIETKSPDTYPGMEEKLIASLQKHKLLGKHS
KPGQVIIQSFSKESLVKVHQLQPNLPTVQLLEAKQMASMTDAALEEIKTY
AVGAGPDYKALNQENVRMIRSHGLLLHPYTVNNEADMHRLLDWGVTGVFT
NYPDLFHKVKKGY
3D structure
PDB5t9c Identification of Two Phosphate Starvation-induced Wall Teichoic Acid Hydrolases Provides First Insights into the Degradative Pathway of a Key Bacterial Cell Wall Component.
ChainE
Resolution1.48 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E70 D72 E152
Catalytic site (residue number reindexed from 1) E40 D42 E122
Enzyme Commision number 3.1.4.46: glycerophosphodiester phosphodiesterase.
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 CA E E70 D72 E152 E40 D42 E122
BS02 G3P E H43 R44 E70 H85 E152 K154 Q188 F190 L210 Y259 F279 H13 R14 E40 H55 E122 K124 Q158 F160 L180 Y229 F249
BS03 PO4 E H43 N281 H13 N251
Gene Ontology
Molecular Function
GO:0008081 phosphoric diester hydrolase activity
GO:0008889 glycerophosphodiester phosphodiesterase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0006071 glycerol metabolic process
GO:0006629 lipid metabolic process
GO:0071555 cell wall organization
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5t9c, PDBe:5t9c, PDBj:5t9c
PDBsum5t9c
PubMed27780866
UniProtP37965|GLPQ_BACSU Glycerophosphodiester phosphodiesterase (Gene Name=glpQ)

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