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1XQ9

Structure of Phosphoglycerate Mutase from Plasmodium falciparum at 2.6 Resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004619molecular_functionphosphoglycerate mutase activity
A0005829cellular_componentcytosol
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0061621biological_processcanonical glycolysis
B0003824molecular_functioncatalytic activity
B0004619molecular_functionphosphoglycerate mutase activity
B0005829cellular_componentcytosol
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0016868molecular_functionintramolecular phosphotransferase activity
B0061621biological_processcanonical glycolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SCN B 500
ChainResidue
BHIS19
BSER22
BTHR31
BARG70

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SCN B 501
ChainResidue
BASN28
BPHE30
BARG124

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SCN A 502
ChainResidue
AARG197
AGLU97
AASN194

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LlRHGEsTwN
ChainResidueDetails
ALEU16-ASN25

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
AGLU97
AHIS192
AHIS19
AARG70

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
BGLU97
BHIS192
BHIS19
BARG70

249697

PDB entries from 2026-02-25

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