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3OZ7

Crystal Structure of 3-Phosphopglycerate Kinase of Plasmodium falciparum

Functional Information from GO Data
ChainGOidnamespacecontents
A0004618molecular_functionphosphoglycerate kinase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016301molecular_functionkinase activity
A0043531molecular_functionADP binding
B0004618molecular_functionphosphoglycerate kinase activity
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016301molecular_functionkinase activity
B0043531molecular_functionADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AGLY213
AALA214
ALYS215
ALYS219

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 601
ChainResidue
AHIS63
AARG66
AARG122
AARG170

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 502
ChainResidue
BALA214
BLYS215
BLYS219
BGLY213

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 602
ChainResidue
BHIS63
BARG66
BARG122

Functional Information from PROSITE/UniProt
site_idPS00111
Number of Residues11
DetailsPGLYCERATE_KINASE Phosphoglycerate kinase signature. KVLVRvDfNVP
ChainResidueDetails
ALYS18-PRO28

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP24
BHIS63
BARG122
BARG170
BGLY312
BGLY372
AARG39
AHIS63
AARG122
AARG170
AGLY312
AGLY372
BASP24
BARG39

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
ALYS215
AGLU343
AASP374
BLYS215
BGLU343
BASP374

219140

PDB entries from 2024-05-01

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