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1YWG

The structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum

Functional Information from GO Data
ChainGOidnamespacecontents
O0000166molecular_functionnucleotide binding
O0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
O0005829cellular_componentcytosol
O0006006biological_processglucose metabolic process
O0006096biological_processglycolytic process
O0016491molecular_functionoxidoreductase activity
O0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
O0050661molecular_functionNADP binding
O0051287molecular_functionNAD binding
P0000166molecular_functionnucleotide binding
P0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
P0005829cellular_componentcytosol
P0006006biological_processglucose metabolic process
P0006096biological_processglycolytic process
P0016491molecular_functionoxidoreductase activity
P0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
P0050661molecular_functionNADP binding
P0051287molecular_functionNAD binding
Q0000166molecular_functionnucleotide binding
Q0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
Q0005829cellular_componentcytosol
Q0006006biological_processglucose metabolic process
Q0006096biological_processglycolytic process
Q0016491molecular_functionoxidoreductase activity
Q0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Q0050661molecular_functionNADP binding
Q0051287molecular_functionNAD binding
R0000166molecular_functionnucleotide binding
R0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
R0005829cellular_componentcytosol
R0006006biological_processglucose metabolic process
R0006096biological_processglycolytic process
R0016491molecular_functionoxidoreductase activity
R0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
R0050661molecular_functionNADP binding
R0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NAD O 401
ChainResidue
OASN9
OPHE37
OGLU79
OLYS80
OSER98
OTHR99
OPHE102
OSER122
OALA123
OCYS153
OTHR183
OGLY10
OALA184
OASN319
OTYR323
OHOH406
OHOH415
OHOH469
OHOH541
OHOH544
OHOH586
OHOH639
OPHE11
OHOH659
OHOH700
OGLY12
OARG13
OILE14
OASN34
OASP35
OPRO36

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NAD P 402
ChainResidue
PASN9
PGLY10
PPHE11
PGLY12
PARG13
PILE14
PASN34
PASP35
PPRO36
PPHE37
PGLU79
PLYS80
PSER98
PTHR99
PPHE102
PSER122
PALA123
PCYS153
PALA184
PASN319
PTYR323
PHOH492
PHOH493
PHOH563
PHOH665
PHOH711

site_idAC3
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NAD Q 403
ChainResidue
PHOH655
QASN9
QGLY10
QPHE11
QGLY12
QARG13
QILE14
QASN34
QASP35
QPRO36
QPHE37
QGLU79
QLYS80
QSER98
QTHR99
QPHE102
QSER122
QALA123
QCYS153
QALA184
QASN319
QTYR323
QHOH429
QHOH436
QHOH498
QHOH511
QHOH716
QHOH831

site_idAC4
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NAD R 404
ChainResidue
RPHE102
RSER122
RALA123
RCYS153
RALA184
RASN319
RTYR323
RHOH442
RHOH471
RHOH577
RHOH734
RHOH736
RHOH789
RASN9
RGLY10
RPHE11
RGLY12
RARG13
RILE14
RASN34
RASP35
RPRO36
RPHE37
RGLU79
RLYS80
RSER98
RTHR99

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
OALA151-LEU158

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. FPCEVTH
ChainResidueDetails
OPHE56-HIS62

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
OHIS180
OCYS153

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
PHIS180
PCYS153

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
QHIS180
QCYS153

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
RHIS180
RCYS153

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PDB entries from 2024-10-09

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