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1NT4

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0006007biological_processglucose catabolic process
A0008877molecular_functionglucose-1-phosphatase activity
A0016158molecular_function3-phytase activity
A0016787molecular_functionhydrolase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0050308molecular_functionsugar-phosphatase activity
B0006007biological_processglucose catabolic process
B0008877molecular_functionglucose-1-phosphatase activity
B0016158molecular_function3-phytase activity
B0016787molecular_functionhydrolase activity
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0050308molecular_functionsugar-phosphatase activity
Functional Information from PROSITE/UniProt
site_idPS00778
Number of Residues17
DetailsHIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. ItVLvGHDSNIasLltA
ChainResidueDetails
AILE283-ALA299

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AALA18
BALA1018

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
AASP290
BASP1290

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING:
ChainResidueDetails
BGLU1196
BHIS1289
AARG17
AARG21
AARG94
AGLU196
AHIS289
BARG1017
BARG1021
BARG1094

221051

PDB entries from 2024-06-12

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