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5DDI

Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from pig muscle - holo enzyme - at 2.40 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
P0000226biological_processmicrotubule cytoskeleton organization
P0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
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
R0000226biological_processmicrotubule cytoskeleton organization
R0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
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
S0000226biological_processmicrotubule cytoskeleton organization
S0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
S0005634cellular_componentnucleus
S0005737cellular_componentcytoplasm
S0005829cellular_componentcytosol
S0005856cellular_componentcytoskeleton
S0006006biological_processglucose metabolic process
S0006096biological_processglycolytic process
S0006417biological_processregulation of translation
S0006915biological_processapoptotic process
S0008017molecular_functionmicrotubule binding
S0015630cellular_componentmicrotubule cytoskeleton
S0016491molecular_functionoxidoreductase activity
S0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
S0016740molecular_functiontransferase activity
S0032481biological_processpositive regulation of type I interferon production
S0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
S0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
S0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
S0045087biological_processinnate immune response
S0050661molecular_functionNADP binding
S0050821biological_processprotein stabilization
S0051287molecular_functionNAD binding
S0051402biological_processneuron apoptotic process
S0097452cellular_componentGAIT complex
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SO4 P 501
ChainResidue
PSER148
PTHR208
PGLY209
PALA210
PHOH620
PHOH640

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 P 502
ChainResidue
PTHR179
PTHR181
PARG231

site_idAC3
Number of Residues16
Detailsbinding site for residue NAD P 503
ChainResidue
PPHE8
PGLY9
PARG10
PILE11
PASP32
PPRO33
PPHE34
PARG77
PTHR96
PGLY97
PSER119
PASN313
PHOH605
PHOH613
PHOH657
RHOH610

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 R 501
ChainResidue
RSER148
RTHR208
RGLY209
RALA210

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 R 502
ChainResidue
RTHR179
RTHR181
RARG231
RNAD503

site_idAC6
Number of Residues13
Detailsbinding site for residue NAD R 503
ChainResidue
RGLY9
RARG10
RILE11
RASN31
RASP32
RPRO33
RARG77
RSER95
RTHR96
RGLY97
RSER119
RASN313
RSO4502

site_idAC7
Number of Residues3
Detailsbinding site for residue SO4 S 501
ChainResidue
STHR208
SGLY209
SALA210

site_idAC8
Number of Residues6
Detailsbinding site for residue SO4 S 502
ChainResidue
STHR179
STHR181
SARG231
SNAD503
SHOH615
SHOH624

site_idAC9
Number of Residues18
Detailsbinding site for residue NAD S 503
ChainResidue
SPHE8
SGLY9
SARG10
SILE11
SASP32
SPRO33
SPHE34
SARG77
STHR96
SGLY97
SSER119
SALA120
SASN313
SSO4502
SHOH620
SHOH624
SHOH625
SHOH666

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
PALA147-LEU154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10009
ChainResidueDetails
PCYS149
RCYS149
SCYS149

site_idSWS_FT_FI2
Number of Residues15
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PARG10
RASN313
SARG10
SASP32
SARG77
SSER119
SASN313
PASP32
PARG77
PSER119
PASN313
RARG10
RASP32
RARG77
RSER119

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P22513
ChainResidueDetails
PSER148
STHR179
STHR208
SARG231
PTHR179
PTHR208
PARG231
RSER148
RTHR179
RTHR208
RARG231
SSER148

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Activates thiol group during catalysis => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PHIS176
RHIS176
SHIS176

site_idSWS_FT_FI5
Number of Residues15
DetailsMOD_RES: N6,N6-dimethyllysine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PLYS2
RLYS331
SLYS2
SLYS63
SGLN257
SLYS260
SLYS331
PLYS63
PGLN257
PLYS260
PLYS331
RLYS2
RLYS63
RGLN257
RLYS260

site_idSWS_FT_FI6
Number of Residues21
DetailsMOD_RES: Deamidated asparagine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PASN6
RASN67
RASN146
RASN152
RASN222
RASN313
SASN6
SASN61
SASN67
SASN146
SASN152
PASN61
SASN222
SASN313
PASN67
PASN146
PASN152
PASN222
PASN313
RASN6
RASN61

site_idSWS_FT_FI7
Number of Residues3
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PTYR39
RTYR39
STYR39

site_idSWS_FT_FI8
Number of Residues9
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PLYS58
PLYS216
PLYS251
RLYS58
RLYS216
RLYS251
SLYS58
SLYS216
SLYS251

site_idSWS_FT_FI9
Number of Residues24
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PTHR72
RTHR150
RTHR174
RTHR179
RTHR181
RTHR208
RTHR226
RTHR234
STHR72
STHR150
STHR174
PTHR150
STHR179
STHR181
STHR208
STHR226
STHR234
PTHR174
PTHR179
PTHR181
PTHR208
PTHR226
PTHR234
RTHR72

site_idSWS_FT_FI10
Number of Residues18
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PSER119
RSER238
RSER309
RSER330
SSER119
SSER145
SSER148
SSER238
SSER309
SSER330
PSER145
PSER148
PSER238
PSER309
PSER330
RSER119
RSER145
RSER148

site_idSWS_FT_FI11
Number of Residues3
DetailsMOD_RES: S-nitrosocysteine; in reversibly inhibited form => ECO:0000250|UniProtKB:P04797
ChainResidueDetails
PCYS149
RCYS149
SCYS149

site_idSWS_FT_FI12
Number of Residues6
DetailsMOD_RES: N6-malonyllysine; alternate => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PLYS191
PLYS212
RLYS191
RLYS212
SLYS191
SLYS212

site_idSWS_FT_FI13
Number of Residues3
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PLYS224
RLYS224
SLYS224

site_idSWS_FT_FI14
Number of Residues3
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PCYS244
RCYS244
SCYS244

site_idSWS_FT_FI15
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P04406
ChainResidueDetails
PLYS183
RLYS183
SLYS183

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PDB entries from 2024-07-24

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