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1LTK

CRYSTAL STRUCTURE OF PHOSPHOGLYCERATE KINASE FROM PLASMODIUM FALCIPARUM, IN THE OPEN CONFORMATION

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004618molecular_functionphosphoglycerate kinase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0043531molecular_functionADP binding
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0004618molecular_functionphosphoglycerate kinase activity
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0043531molecular_functionADP binding
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0004618molecular_functionphosphoglycerate kinase activity
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0006094biological_processgluconeogenesis
C0006096biological_processglycolytic process
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0043531molecular_functionADP binding
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 604
ChainResidue
CASN26
CARG66
CARG122
CLYS138
CARG170

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 605
ChainResidue
AHIS63
AARG66
AARG122
AARG170

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 606
ChainResidue
BASN26
BHIS63
BARG66
BARG122
BARG170

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AMP A 501
ChainResidue
AGLY213
AALA214
ALYS215
AGLY237
AGLY238
ALEU256
AGLY340
AVAL341
AGLU343
AASP374
BLYS140
BLYS143

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AMP B 502
ChainResidue
ALYS143
BGLY213
BALA214
BLYS215
BLYS219
BGLY237
BGLY238
BLEU313
BGLY340
BVAL341
BGLU343
BASP374

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE AMP C 503
ChainResidue
CLYS140
CLYS143
CGLY213
CALA214
CLYS215
CGLY237
CGLY238
CLEU256
CGLY340
CGLU343
CASP374

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 614
ChainResidue
AASN72
ALYS74
ATYR75
BLYS74

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 Residues39
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00558","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues39
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q7SIB7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 13pk
ChainResidueDetails
ALYS215
AARG39
AGLY373
AGLY396

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 13pk
ChainResidueDetails
BLYS215
BARG39
BGLY373
BGLY396

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 13pk
ChainResidueDetails
CLYS215
CARG39
CGLY373
CGLY396

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PDB entries from 2025-10-22

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