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1GAD

COMPARISON OF THE STRUCTURES OF WILD TYPE AND A N313T MUTANT OF ESCHERICHIA COLI GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASES: IMPLICATION FOR NAD BINDING AND COOPERATIVITY

Functional Information from GO Data
ChainGOidnamespacecontents
O0000166molecular_functionnucleotide binding
O0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
O0005515molecular_functionprotein binding
O0005737cellular_componentcytoplasm
O0005829cellular_componentcytosol
O0006006biological_processglucose metabolic process
O0006096biological_processglycolytic process
O0016020cellular_componentmembrane
O0016491molecular_functionoxidoreductase activity
O0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
O0042802molecular_functionidentical protein binding
O0050661molecular_functionNADP binding
O0051287molecular_functionNAD binding
P0000166molecular_functionnucleotide binding
P0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
P0005515molecular_functionprotein binding
P0005737cellular_componentcytoplasm
P0005829cellular_componentcytosol
P0006006biological_processglucose metabolic process
P0006096biological_processglycolytic process
P0016020cellular_componentmembrane
P0016491molecular_functionoxidoreductase activity
P0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
P0042802molecular_functionidentical protein binding
P0050661molecular_functionNADP binding
P0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE NAD O 336
ChainResidue
OGLY9
OLEU98
OTHR119
OCYS149
OASN313
OTYR317
OHOH344
OHOH345
OHOH347
OHOH356
OHOH359
OARG10
OHOH366
OHOH383
OHOH384
OHOH460
OILE11
OASN31
OASP32
OARG77
OALA95
OTHR96
OGLY97

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE NAD P 336
ChainResidue
PGLY7
PGLY9
PARG10
PILE11
PASN31
PASP32
PARG77
PALA95
PTHR96
PGLY97
PLEU98
PTHR119
PALA180
PASN313
PTYR317
PHOH350
PHOH351
PHOH353
PHOH366
PHOH372
PHOH378
PHOH394
PHOH421
PHOH456
PHOH483

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
OALA147-LEU154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:10978154
ChainResidueDetails
OTHR150
PTHR150

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984, ECO:0000269|Ref.18
ChainResidueDetails
OILE11
PILE11

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984
ChainResidueDetails
OLEU33
OGLU314
PLEU33
PGLU314

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219
ChainResidueDetails
OASP78
PASP78

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19542219
ChainResidueDetails
OGLY120
PGLY120

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10978154
ChainResidueDetails
OCYS149
OGLY209
PCYS149
PGLY209

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00362
ChainResidueDetails
OALA180
PALA180

site_idSWS_FT_FI8
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19542219, ECO:0000269|Ref.18, ECO:0000305|PubMed:10978154
ChainResidueDetails
OVAL232
PVAL232

site_idSWS_FT_FI9
Number of Residues2
DetailsSITE: Activates thiol group during catalysis => ECO:0000269|PubMed:2659073
ChainResidueDetails
OALA177
PALA177

site_idSWS_FT_FI10
Number of Residues16
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122
ChainResidueDetails
OLYS115
PASP123
PALA213
PVAL217
PLEU225
PALA249
PALA257
PALA261
OASP123
OALA213
OVAL217
OLEU225
OALA249
OALA257
OALA261
PLYS115

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122
ChainResidueDetails
OGLY131
OASP192
PGLY131
PASP192

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
OTYR137
PTYR137

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
OCYS149
OHIS176

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
PCYS149
PHIS176

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PDB entries from 2024-07-24

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