1NT4

Crystal structure of Escherichia coli periplasmic glucose-1-phosphatase H18A mutant complexed with glucose-1-phosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006007	biological_process	glucose catabolic process
A	0008877	molecular_function	glucose-1-phosphatase activity
A	0016158	molecular_function	inositol hexakisphosphate 3-phosphatase activity
A	0016787	molecular_function	hydrolase activity
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0042597	cellular_component	periplasmic space
A	0050308	molecular_function	sugar-phosphatase activity
B	0006007	biological_process	glucose catabolic process
B	0008877	molecular_function	glucose-1-phosphatase activity
B	0016158	molecular_function	inositol hexakisphosphate 3-phosphatase activity
B	0016787	molecular_function	hydrolase activity
B	0030288	cellular_component	outer membrane-bounded periplasmic space
B	0042597	cellular_component	periplasmic space
B	0050308	molecular_function	sugar-phosphatase activity

Functional Information from PROSITE/UniProt

site_id	PS00778
Number of Residues	17
Details	HIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. ItVLvGHDSNIasLltA

Chain	Residue	Details
A	ILE283-ALA299

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Nucleophile"}

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Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor"}

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Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {}

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Residue

Details

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