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1J0X

Crystal structure of the rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH)

Functional Information from GO Data
ChainGOidnamespacecontents
O0000226biological_processmicrotubule cytoskeleton organization
O0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
O0005515molecular_functionprotein binding
O0005634cellular_componentnucleus
O0005737cellular_componentcytoplasm
O0005829cellular_componentcytosol
O0005856cellular_componentcytoskeleton
O0006006biological_processglucose metabolic process
O0006096biological_processglycolytic process
O0006417biological_processregulation of translation
O0006915biological_processapoptotic process
O0008017molecular_functionmicrotubule binding
O0015630cellular_componentmicrotubule cytoskeleton
O0016491molecular_functionoxidoreductase activity
O0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
O0016740molecular_functiontransferase activity
O0032481biological_processpositive regulation of type I interferon production
O0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
O0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
O0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
O0045087biological_processinnate immune response
O0050661molecular_functionNADP binding
O0050821biological_processprotein stabilization
O0051287molecular_functionNAD binding
O0051402biological_processneuron apoptotic process
O0097452cellular_componentGAIT complex
P0000226biological_processmicrotubule cytoskeleton organization
P0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
P0005515molecular_functionprotein binding
P0005634cellular_componentnucleus
P0005737cellular_componentcytoplasm
P0005829cellular_componentcytosol
P0005856cellular_componentcytoskeleton
P0006006biological_processglucose metabolic process
P0006096biological_processglycolytic process
P0006417biological_processregulation of translation
P0006915biological_processapoptotic process
P0008017molecular_functionmicrotubule binding
P0015630cellular_componentmicrotubule cytoskeleton
P0016491molecular_functionoxidoreductase activity
P0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
P0016740molecular_functiontransferase activity
P0032481biological_processpositive regulation of type I interferon production
P0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
P0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
P0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
P0045087biological_processinnate immune response
P0050661molecular_functionNADP binding
P0050821biological_processprotein stabilization
P0051287molecular_functionNAD binding
P0051402biological_processneuron apoptotic process
P0097452cellular_componentGAIT complex
Q0000226biological_processmicrotubule cytoskeleton organization
Q0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
Q0005515molecular_functionprotein binding
Q0005634cellular_componentnucleus
Q0005737cellular_componentcytoplasm
Q0005829cellular_componentcytosol
Q0005856cellular_componentcytoskeleton
Q0006006biological_processglucose metabolic process
Q0006096biological_processglycolytic process
Q0006417biological_processregulation of translation
Q0006915biological_processapoptotic process
Q0008017molecular_functionmicrotubule binding
Q0015630cellular_componentmicrotubule cytoskeleton
Q0016491molecular_functionoxidoreductase activity
Q0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Q0016740molecular_functiontransferase activity
Q0032481biological_processpositive regulation of type I interferon production
Q0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
Q0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
Q0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
Q0045087biological_processinnate immune response
Q0050661molecular_functionNADP binding
Q0050821biological_processprotein stabilization
Q0051287molecular_functionNAD binding
Q0051402biological_processneuron apoptotic process
Q0097452cellular_componentGAIT complex
R0000226biological_processmicrotubule cytoskeleton organization
R0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
R0005515molecular_functionprotein binding
R0005634cellular_componentnucleus
R0005737cellular_componentcytoplasm
R0005829cellular_componentcytosol
R0005856cellular_componentcytoskeleton
R0006006biological_processglucose metabolic process
R0006096biological_processglycolytic process
R0006417biological_processregulation of translation
R0006915biological_processapoptotic process
R0008017molecular_functionmicrotubule binding
R0015630cellular_componentmicrotubule cytoskeleton
R0016491molecular_functionoxidoreductase activity
R0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
R0016740molecular_functiontransferase activity
R0032481biological_processpositive regulation of type I interferon production
R0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
R0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
R0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
R0045087biological_processinnate immune response
R0050661molecular_functionNADP binding
R0050821biological_processprotein stabilization
R0051287molecular_functionNAD binding
R0051402biological_processneuron apoptotic process
R0097452cellular_componentGAIT complex
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NAD P 1336
ChainResidue
PASN6
PARG77
PSER95
PTHR96
PGLY97
PPHE99
PSER119
PALA120
PCSX149
PASN313
PTYR317
PPHE8
PHOH1375
PGLY9
PARG10
PILE11
PASP32
PPRO33
PPHE34
PILE35

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAD R 2336
ChainResidue
OHOH363
RASN6
RPHE8
RGLY9
RARG10
RILE11
RASP32
RPRO33
RPHE34
RILE35
RARG77
RSER95
RTHR96
RGLY97
RPHE99
RSER119
RALA120
RCSX149
RASN313
RTYR317
RHOH2428

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 Residues4
DetailsACT_SITE: Nucleophile
ChainResidueDetails
OTHR150
PTHR150
QTHR150
RTHR150

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:14646080
ChainResidueDetails
OILE11
QPRO33
QASP78
QGLU314
RILE11
RPRO33
RASP78
RGLU314
OPRO33
OASP78
OGLU314
PILE11
PPRO33
PASP78
PGLU314
QILE11

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
OALA120
PALA120
QALA120
RALA120

site_idSWS_FT_FI4
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P22513
ChainResidueDetails
OCSX149
QALA180
QGLY209
QVAL232
RCSX149
RALA180
RGLY209
RVAL232
OALA180
OGLY209
OVAL232
PCSX149
PALA180
PGLY209
PVAL232
QCSX149

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Activates thiol group during catalysis => ECO:0000305|PubMed:14646080
ChainResidueDetails
OALA177
PALA177
QALA177
RALA177

site_idSWS_FT_FI6
Number of Residues20
DetailsMOD_RES: N6,N6-dimethyllysine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
OVAL3
PGLU332
QVAL3
QLEU64
QVAL258
QGLN261
QGLU332
RVAL3
RLEU64
RVAL258
RGLN261
OLEU64
RGLU332
OVAL258
OGLN261
OGLU332
PVAL3
PLEU64
PVAL258
PGLN261

site_idSWS_FT_FI7
Number of Residues28
DetailsMOD_RES: Deamidated asparagine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
OGLY7
PGLY68
PALA147
PCYS153
PGLY223
PGLU314
QGLY7
QGLY62
QGLY68
QALA147
QCYS153
OGLY62
QGLY223
QGLU314
RGLY7
RGLY62
RGLY68
RALA147
RCYS153
RGLY223
RGLU314
OGLY68
OALA147
OCYS153
OGLY223
OGLU314
PGLY7
PGLY62

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
OMET40
PMET40
QMET40
RMET40

site_idSWS_FT_FI9
Number of Residues12
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
OALA59
RALA59
RVAL217
RTYR252
OVAL217
OTYR252
PALA59
PVAL217
PTYR252
QALA59
QVAL217
QTYR252

site_idSWS_FT_FI10
Number of Residues32
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
OILE73
PTHR151
PVAL175
PALA180
PGLN182
PGLY209
PGLY227
PPRO235
QILE73
QTHR151
QVAL175
OTHR151
QALA180
QGLN182
QGLY209
QGLY227
QPRO235
RILE73
RTHR151
RVAL175
RALA180
RGLN182
OVAL175
RGLY209
RGLY227
RPRO235
OALA180
OGLN182
OGLY209
OGLY227
OPRO235
PILE73

site_idSWS_FT_FI11
Number of Residues24
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
OALA120
PVAL239
PTRP310
PLYS331
QALA120
QASN146
QCSX149
QVAL239
QTRP310
QLYS331
RALA120
OASN146
RASN146
RCSX149
RVAL239
RTRP310
RLYS331
OCSX149
OVAL239
OTRP310
OLYS331
PALA120
PASN146
PCSX149

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: S-nitrosocysteine; in reversibly inhibited form => ECO:0000250|UniProtKB:P04797
ChainResidueDetails
OTHR150
PTHR150
QTHR150
RTHR150

site_idSWS_FT_FI13
Number of Residues8
DetailsMOD_RES: N6-malonyllysine; alternate => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
OLEU192
OALA213
PLEU192
PALA213
QLEU192
QALA213
RLEU192
RALA213

site_idSWS_FT_FI14
Number of Residues4
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
OLEU225
PLEU225
QLEU225
RLEU225

site_idSWS_FT_FI15
Number of Residues4
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
OARG245
PARG245
QARG245
RARG245

site_idSWS_FT_FI16
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
OTHR184
PTHR184
QTHR184
RTHR184

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
OHIS176

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
PHIS176

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
QHIS176

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
RHIS176

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PDB entries from 2024-07-17

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