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2B4R

Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum at 2.25 Angstrom Resolution reveals intriguing extra electron density in the active site

Replaces:  1ZYA
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 Residues25
DetailsBINDING SITE FOR RESIDUE NAD Q 501
ChainResidue
PHOH767
QSER98
QTHR99
QGLY100
QPHE102
QSER122
QALA123
QCYS153
QTHR183
QALA184
QASN319
QGLY10
QTYR323
QHOH513
QHOH522
QHOH523
QHOH549
QHOH550
QPHE11
QGLY12
QARG13
QILE14
QASP35
QPRO36
QPHE37

site_idAC2
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NAD P 701
ChainResidue
PASN9
PGLY10
PGLY12
PARG13
PILE14
PASN34
PASP35
PPRO36
PPHE37
PLYS80
PSER98
PTHR99
PGLY100
PSER122
PALA123
PCYS153
PALA184
PASN319
PTYR323
PAES602
PHOH707
PHOH711
PHOH720
PHOH727
PHOH732
PHOH740
PHOH754

site_idAC3
Number of Residues29
DetailsBINDING SITE FOR RESIDUE NAD O 801
ChainResidue
OASN9
OGLY10
OPHE11
OGLY12
OARG13
OILE14
OASN34
OASP35
OPRO36
OPHE37
OMET38
OGLU79
OLYS80
OSER98
OTHR99
OGLY100
OSER122
OALA123
OCYS153
OALA184
OASN319
OTYR323
OAES601
OHOH812
OHOH829
OHOH842
OHOH847
OHOH853
RHOH963

site_idAC4
Number of Residues29
DetailsBINDING SITE FOR RESIDUE NAD R 901
ChainResidue
RASN319
RTYR323
RAES603
RHOH904
RHOH907
RHOH910
RHOH918
RHOH923
RHOH939
RHOH941
RHOH942
RASN9
RGLY10
RGLY12
RARG13
RILE14
RASN34
RASP35
RPRO36
RPHE37
RGLU79
RLYS80
RSER98
RTHR99
RGLY100
RPHE102
RSER122
RALA123
RALA184

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE AES O 601
ChainResidue
OTHR183
OASN185
ONAD801

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE AES P 602
ChainResidue
PTHR183
PASN185
PARG237
PNAD701

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE AES R 603
ChainResidue
RTHR183
RASN185
RNAD901

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL R 503
ChainResidue
QGLY196
QLYS197
QASP198
QTRP199
RGLU283

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL P 703
ChainResidue
OGLU283
PGLY196
PASP198
PTRP199

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL O 804
ChainResidue
OASP292
OASN293
OARG294
RGLU71

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL R 903
ChainResidue
QGLU283
RASP198
RTRP199

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

218853

PDB entries from 2024-04-24

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