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2HF2

Domain shifting confirms monomeric structure of Escherichia sugar phosphatase SUPH

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005829cellular_componentcytosol
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0046872molecular_functionmetal ion binding
A0050286molecular_functionsorbitol-6-phosphatase activity
A0050308molecular_functionsugar-phosphatase activity
A0103026molecular_functionfructose-1-phosphatase activity
B0000287molecular_functionmagnesium ion binding
B0005829cellular_componentcytosol
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0046872molecular_functionmetal ion binding
B0050286molecular_functionsorbitol-6-phosphatase activity
B0050308molecular_functionsugar-phosphatase activity
B0103026molecular_functionfructose-1-phosphatase activity
Functional Information from PROSITE/UniProt
site_idPS01229
Number of Residues23
DetailsCOF_2 Hypothetical cof family signature 2. IGDSgNDaemLkmArySfaMgnA
ChainResidueDetails
AILE213-ALA235

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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