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2X0N

Structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei determined from Laue data

Replaces:  1GGA
Functional Information from GO Data
ChainGOidnamespacecontents
A0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0006006biological_processglucose metabolic process
A0006096biological_processglycolytic process
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0020015cellular_componentglycosome
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
B0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
B0005777cellular_componentperoxisome
B0005829cellular_componentcytosol
B0006006biological_processglucose metabolic process
B0006096biological_processglycolytic process
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0020015cellular_componentglycosome
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
O0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
O0005777cellular_componentperoxisome
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
O0020015cellular_componentglycosome
O0050661molecular_functionNADP binding
O0051287molecular_functionNAD binding
P0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
P0005777cellular_componentperoxisome
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
P0020015cellular_componentglycosome
P0050661molecular_functionNADP binding
P0051287molecular_functionNAD binding
Q0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
Q0005777cellular_componentperoxisome
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
Q0020015cellular_componentglycosome
Q0050661molecular_functionNADP binding
Q0051287molecular_functionNAD binding
R0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
R0005777cellular_componentperoxisome
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
R0020015cellular_componentglycosome
R0050661molecular_functionNADP binding
R0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 359
ChainResidue
ATHR196
ATHR198
ANAD361

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 360
ChainResidue
ASER164
ATHR225
AGLY226
AALA227

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAD A 361
ChainResidue
AARG11
AILE12
AASP37
AMET38
AALA89
AGLN90
ASER109
ATHR110
AGLY111
ALEU112
ASER133
AALA134
ACYS165
AALA197
AASN334
ASO4359
AGLY8
AGLY10

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 359
ChainResidue
BTHR196
BTHR198
BARG248

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 360
ChainResidue
BSER164
BTHR225
BGLY226
BALA227

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE NAD B 361
ChainResidue
BASN7
BGLY8
BGLY10
BARG11
BILE12
BASP37
BMET38
BALA89
BGLN90
BSER109
BTHR110
BGLY111
BLEU112
BSER133
BALA134
BALA197
BASN334

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 O 359
ChainResidue
OTHR196
OTHR198
OARG248

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 O 360
ChainResidue
OSER164
OTHR225
OGLY226
OALA227

site_idAC9
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NAD O 361
ChainResidue
OGLY8
OGLY10
OARG11
OILE12
OASP37
OALA89
OGLN90
OSER109
OTHR110
OGLY111
OSER133
OALA134
OCYS165
OALA197
OASN334
OTYR338

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 P 359
ChainResidue
PTHR196
PTHR198
PARG248

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 P 360
ChainResidue
PSER164
PTHR225

site_idBC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE NAD P 361
ChainResidue
PGLY8
PGLY10
PARG11
PILE12
PVAL36
PASP37
PMET38
PALA89
PGLN90
PSER109
PTHR110
PGLY111
PSER133
PASN334
PTYR338

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 Q 359
ChainResidue
QTHR196
QTHR198
QARG248

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 Q 360
ChainResidue
QSER164
QTHR225
QGLY226
QALA227

site_idBC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NAD Q 361
ChainResidue
QGLY8
QGLY10
QARG11
QILE12
QVAL36
QASP37
QMET38
QGLN90
QSER109
QTHR110
QGLY111
QSER133
QCYS165
QALA197
QASN334
QTYR338

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 R 359
ChainResidue
RTHR196
RTHR198
RARG248
RNAD361

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 R 360
ChainResidue
RSER164
RTHR225
RGLY226
RALA227

site_idBC9
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAD R 361
ChainResidue
RGLY8
RGLY10
RARG11
RILE12
RVAL36
RASP37
RMET38
RALA89
RGLN90
RSER109
RTHR110
RSER133
RALA134
RCYS165
RALA197
RASN334
RTYR338
RSO4359

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
AALA163-LEU170

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10009
ChainResidueDetails
ACYS165
BCYS165
OCYS165
PCYS165
QCYS165
RCYS165

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:8460146
ChainResidueDetails
AARG11
OASP37
OGLN90
OASN334
PARG11
PASP37
PGLN90
PASN334
QARG11
QASP37
QGLN90
AASP37
QASN334
RARG11
RASP37
RGLN90
RASN334
AGLN90
AASN334
BARG11
BASP37
BGLN90
BASN334
OARG11

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER164
OTHR196
OTHR225
OARG248
PSER164
PTHR196
PTHR225
PARG248
QSER164
QTHR196
QTHR225
ATHR196
QARG248
RSER164
RTHR196
RTHR225
RARG248
ATHR225
AARG248
BSER164
BTHR196
BTHR225
BARG248
OSER164

site_idSWS_FT_FI4
Number of Residues6
DetailsSITE: Activates thiol group during catalysis => ECO:0000250
ChainResidueDetails
AHIS193
BHIS193
OHIS193
PHIS193
QHIS193
RHIS193

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
AHIS193
ACYS165

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
BHIS193
BCYS165

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
OHIS193
OCYS165

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
PHIS193
PCYS165

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
QHIS193
QCYS165

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
RHIS193
RCYS165

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PDB entries from 2025-07-02

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