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

1LTK

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

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
C0004618molecular_functionphosphoglycerate kinase activity
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0006094biological_processgluconeogenesis
C0006096biological_processglycolytic process
C0016301molecular_functionkinase activity
C0043531molecular_functionADP 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 Residues21
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP24
BHIS63
BARG122
BARG170
BGLY312
BGLY372
CASP24
CARG39
CHIS63
CARG122
CARG170
AARG39
CGLY312
CGLY372
AHIS63
AARG122
AARG170
AGLY312
AGLY372
BASP24
BARG39

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING:
ChainResidueDetails
ALYS215
AGLU343
AASP374
BLYS215
BGLU343
BASP374
CLYS215
CGLU343
CASP374

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

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon