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2B0C

The crystal structure of the putative phosphatase from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0008877molecular_functionglucose-1-phosphatase activity
A0016787molecular_functionhydrolase activity
A0030145molecular_functionmanganese ion binding
A0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2011","submissionDatabase":"PDB data bank","title":"The 2.0a crystal structure of the putative phosphatase from Escherichia coli.","authoringGroup":["Midwest center for structural genomics (MCSG)"]}}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1lvh
ChainResidueDetails
ASER114
ALYS148

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1lvh
ChainResidueDetails
AASP13
AARG35
ASER114
AASN177

239492

PDB entries from 2025-07-30

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