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1NQ5

Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ser Complexed With Nad+

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A0005737cellular_componentcytoplasm
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
A0030554molecular_functionadenyl nucleotide binding
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
C0000166molecular_functionnucleotide binding
C0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
C0005737cellular_componentcytoplasm
C0006006biological_processglucose metabolic process
C0006096biological_processglycolytic process
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0030554molecular_functionadenyl nucleotide binding
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
O0000166molecular_functionnucleotide binding
O0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
O0005737cellular_componentcytoplasm
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
O0030554molecular_functionadenyl nucleotide binding
O0050661molecular_functionNADP binding
O0051287molecular_functionNAD binding
Q0000166molecular_functionnucleotide binding
Q0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
Q0005737cellular_componentcytoplasm
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
Q0030554molecular_functionadenyl nucleotide binding
Q0050661molecular_functionNADP binding
Q0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 O 1338
ChainResidue
OTHR179
OASP181
OARG195
OARG231
ONAD1336
OHOH1407
OHOH1453
OHOH1465

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 Q 3338
ChainResidue
QASP181
QARG195
QARG231
QHOH1468
QNAD3336
QTHR179

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 5338
ChainResidue
ATHR179
AASP181
AARG195
AARG231
AHOH1471
ANAD5336

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 7338
ChainResidue
CTHR179
CASP181
CARG195
CARG231
CNAD7336
CHOH7479

site_idAC5
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NAD O 1336
ChainResidue
OGLY7
OGLY9
OARG10
OILE11
OASN31
OASP32
OGLU76
OARG77
OSER95
OTHR96
OGLY97
OPHE99
OSER119
OALA120
OTHR179
OASN180
OASN313
OTYR317
OSO41338
OHOH1341
OHOH1356
OHOH1360
OHOH1361
OHOH1382
OHOH1441
OHOH1450
OHOH1453
OHOH1466
OHOH1467
QLEU187
QHOH3426

site_idAC6
Number of Residues29
DetailsBINDING SITE FOR RESIDUE NAD Q 3336
ChainResidue
OLEU187
OHOH1389
OHOH1457
QGLY7
QGLY9
QARG10
QILE11
QASN31
QASP32
QLEU33
QGLU76
QARG77
QSER95
QTHR96
QGLY97
QPHE99
QSER119
QALA120
QASN180
QASN313
QTYR317
QHOH1468
QSO43338
QHOH3342
QHOH3374
QHOH3385
QHOH3419
QHOH3482
QHOH3499

site_idAC7
Number of Residues30
DetailsBINDING SITE FOR RESIDUE NAD A 5336
ChainResidue
APHE99
ASER119
AALA120
ATHR179
AASN180
ALEU187
AASN313
AHOH1471
AHOH1473
AHOH1474
ASO45338
AHOH5342
AHOH5365
AHOH5366
AHOH5393
AHOH5458
AHOH5468
AGLY7
AGLY9
AARG10
AILE11
AASN31
AASP32
ALEU33
AGLU76
AARG77
ASER95
ATHR96
AGLY97
AARG98

site_idAC8
Number of Residues29
DetailsBINDING SITE FOR RESIDUE NAD C 7336
ChainResidue
CGLY7
CGLY9
CARG10
CILE11
CASN31
CASP32
CLEU33
CARG77
CSER95
CTHR96
CGLY97
CARG98
CSER119
CALA120
CASN180
CASN313
CTYR317
CSO47338
CHOH7342
CHOH7365
CHOH7373
CHOH7374
CHOH7376
CHOH7403
CHOH7411
CHOH7467
CHOH7473
CHOH7479
CHOH7482

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:18480053, ECO:0000305|PubMed:12569100
ChainResidueDetails
OTHR150
QTHR150
ATHR150
CTHR150

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858
ChainResidueDetails
OILE11
QALA120
QASP181
QGLU314
AILE11
ALEU33
AASP78
AALA120
AASP181
AGLU314
CILE11
OLEU33
CLEU33
CASP78
CALA120
CASP181
CGLU314
OASP78
OALA120
OASP181
OGLU314
QILE11
QLEU33
QASP78

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3210237, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858
ChainResidueDetails
OSER149
CSER149
CASN180
CVAL232
OASN180
OVAL232
QSER149
QASN180
QVAL232
ASER149
AASN180
AVAL232

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:9175858
ChainResidueDetails
OALA196
QALA196
AALA196
CALA196

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3210237, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858
ChainResidueDetails
OGLY209
QGLY209
AGLY209
CGLY209

site_idSWS_FT_FI6
Number of Residues4
DetailsSITE: Activates thiol group during catalysis => ECO:0000250|UniProtKB:Q6GIL8
ChainResidueDetails
OSER177
QSER177
ASER177
CSER177

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
OSER149
OHIS176

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
QSER149
QHIS176

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
ASER149
AHIS176

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
CSER149
CHIS176

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PDB entries from 2025-06-18

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