Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
DetailsACT_SITE: Nucleophile => ECO:0000255
ChainResidueDetails
AASP9
BASP9

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING:
ChainResidueDetails
AASP9
BASP11
BSER44
BLYS192
BASP215
BSER216
AMSE10
AASP11
ASER44
ALYS192
AASP215
ASER216
BASP9
BMSE10

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASN218
BASN218

225946

PDB entries from 2024-10-09

PDB statisticsPDBj update infoContact PDBjnumon