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4QJB

Crystal structure of the sugar phosphatase PfHAD1 from Plasmodium falciparum

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0010323biological_processnegative regulation of isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
A0016311biological_processdephosphorylation
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0050308molecular_functionsugar-phosphatase activity
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0010323biological_processnegative regulation of isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
B0016311biological_processdephosphorylation
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0050308molecular_functionsugar-phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 301
ChainResidue
AASP27
AASP29
AASP238
AHOH451

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 302
ChainResidue
AASP27
AGLY62
ALYS215
AASN241

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 301
ChainResidue
BASP29
BASP238
BASP27

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 302
ChainResidue
BASP27
BASP29
BTHR61

Functional Information from PROSITE/UniProt
site_idPS01228
Number of Residues12
DetailsCOF_1 Hypothetical cof family signature 1. IIftDLDGTLLN
ChainResidueDetails
AILE23-ASN34

221051

PDB entries from 2024-06-12

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