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3GPD

TWINNING IN CRYSTALS OF HUMAN SKELETAL MUSCLE D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE

Functional Information from GO Data
ChainGOidnamespacecontents
G0000226biological_processmicrotubule cytoskeleton organization
G0001819biological_processpositive regulation of cytokine production
G0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005737cellular_componentcytoplasm
G0005811cellular_componentlipid droplet
G0005829cellular_componentcytosol
G0005856cellular_componentcytoskeleton
G0005886cellular_componentplasma membrane
G0006006biological_processglucose metabolic process
G0006096biological_processglycolytic process
G0006417biological_processregulation of translation
G0006915biological_processapoptotic process
G0008017molecular_functionmicrotubule binding
G0010951biological_processnegative regulation of endopeptidase activity
G0015630cellular_componentmicrotubule cytoskeleton
G0016020cellular_componentmembrane
G0016241biological_processregulation of macroautophagy
G0016491molecular_functionoxidoreductase activity
G0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
G0016740molecular_functiontransferase activity
G0017148biological_processnegative regulation of translation
G0019828molecular_functionaspartic-type endopeptidase inhibitor activity
G0031640biological_processkilling of cells of another organism
G0031965cellular_componentnuclear membrane
G0031982cellular_componentvesicle
G0032481biological_processpositive regulation of type I interferon production
G0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
G0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
G0042802molecular_functionidentical protein binding
G0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
G0043231cellular_componentintracellular membrane-bounded organelle
G0045087biological_processinnate immune response
G0048471cellular_componentperinuclear region of cytoplasm
G0050661molecular_functionNADP binding
G0050821biological_processprotein stabilization
G0050832biological_processdefense response to fungus
G0051287molecular_functionNAD binding
G0051402biological_processneuron apoptotic process
G0051873biological_processkilling by host of symbiont cells
G0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
G0070062cellular_componentextracellular exosome
G0071346biological_processcellular response to type II interferon
G0097452cellular_componentGAIT complex
G0097718molecular_functiondisordered domain specific binding
G1990904cellular_componentribonucleoprotein complex
R0000226biological_processmicrotubule cytoskeleton organization
R0001819biological_processpositive regulation of cytokine production
R0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
R0005515molecular_functionprotein binding
R0005634cellular_componentnucleus
R0005737cellular_componentcytoplasm
R0005811cellular_componentlipid droplet
R0005829cellular_componentcytosol
R0005856cellular_componentcytoskeleton
R0005886cellular_componentplasma membrane
R0006006biological_processglucose metabolic process
R0006096biological_processglycolytic process
R0006417biological_processregulation of translation
R0006915biological_processapoptotic process
R0008017molecular_functionmicrotubule binding
R0010951biological_processnegative regulation of endopeptidase activity
R0015630cellular_componentmicrotubule cytoskeleton
R0016020cellular_componentmembrane
R0016241biological_processregulation of macroautophagy
R0016491molecular_functionoxidoreductase activity
R0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
R0016740molecular_functiontransferase activity
R0017148biological_processnegative regulation of translation
R0019828molecular_functionaspartic-type endopeptidase inhibitor activity
R0031640biological_processkilling of cells of another organism
R0031965cellular_componentnuclear membrane
R0031982cellular_componentvesicle
R0032481biological_processpositive regulation of type I interferon production
R0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
R0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
R0042802molecular_functionidentical protein binding
R0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
R0043231cellular_componentintracellular membrane-bounded organelle
R0045087biological_processinnate immune response
R0048471cellular_componentperinuclear region of cytoplasm
R0050661molecular_functionNADP binding
R0050821biological_processprotein stabilization
R0050832biological_processdefense response to fungus
R0051287molecular_functionNAD binding
R0051402biological_processneuron apoptotic process
R0051873biological_processkilling by host of symbiont cells
R0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
R0070062cellular_componentextracellular exosome
R0071346biological_processcellular response to type II interferon
R0097452cellular_componentGAIT complex
R0097718molecular_functiondisordered domain specific binding
R1990904cellular_componentribonucleoprotein complex
Functional Information from PDB Data
site_idABR
Number of Residues8
DetailsRESIDUES INTERACTING WITH THE ADENINE BASE OF THE NAD COFACTOR IN THE RED SUBUNIT
ChainResidue
RASP8
RGLY9
RASN33
RASP34
RPRO35
RGLU78
RARG79
RASP80

site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 R 338
ChainResidue
RTHR181
RTHR183
RNAD336

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 R 340
ChainResidue
RSER150
RCYS151
RTHR210
RGLY211

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 G 338
ChainResidue
GTHR181
GTHR183
GNAD336

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 G 340
ChainResidue
GSER150
GCYS151
GTHR152
GTHR210
GGLY211

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NAD R 336
ChainResidue
RGLY9
RGLY11
RARG12
RILE13
RASN33
RASP34
RPRO35
RPHE36
RGLU78
RASP80
RSER97
RTHR98
RSER121
RALA122
RCYS151
RILE180
RALA182
RASN315
RGLU316
RSO4338

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NAD G 336
ChainResidue
GGLY9
GGLY11
GARG12
GILE13
GPRO35
GARG79
GSER97
GTHR98
GGLY99
GPHE101
GSER121
GALA122
GCYS151
GALA182
GASN315
GSO4338

site_idAPR
Number of Residues2
DetailsRESIDUES INTERACTING WITH THE PHOSPHATE OF THE ADENOSINE NUCLEOTIDE OF THE NAD COFACTOR IN THE RED SUBUNIT
ChainResidue
RGLY11
RARG12

site_idARR
Number of Residues3
DetailsRESIDUES INTERACTING WITH THE ADENOSINE RIBOSE OF THE NAD COFACTOR IN THE RED SUBUNIT
ChainResidue
RSER97
RTHR98
RPHE36

site_idIPR
Number of Residues4
DetailsRESIDUES INTERACTING WITH THE SUBSTRATE AND THE INORGANIC PHOSPHATE GROUPS RESPECTIVELY OF THE RED SUBUNIT
ChainResidue
RTHR181
RALA182
RTHR183
RARG233

site_idNBR
Number of Residues4
DetailsRESIDUES INTERACTING WITH THE NICOTINAMIDE BASE OF THE NAD COFACTOR IN THE RED SUBUNIT
ChainResidue
RCYS151
RILE180
RASN315
RGLU316

site_idNPR
Number of Residues2
DetailsRESIDUES INTERACTING WITH THE PHOSPHATE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR IN THE RED SUBUNIT
ChainResidue
RARG12
RILE13

site_idNRR
Number of Residues3
DetailsRESIDUES INTERACTING WITH THE RIBOSE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR IN THE RED SUBUNIT
ChainResidue
RILE13
RSER121
RALA122

site_idSPR
Number of Residues4
DetailsRESIDUES INTERACTING WITH THE SUBSTRATE AND THE INORGANIC PHOSPHATE GROUPS RESPECTIVELY OF THE RED SUBUNIT
ChainResidue
RSER150
RCYS151
RTHR152
RTHR210

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
RALA149-LEU156

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:25086035
ChainResidueDetails
RTHR152
GTHR152

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976
ChainResidueDetails
RILE13
GGLU316
RPRO35
RASP80
RALA122
RGLU316
GILE13
GPRO35
GASP80
GALA122

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P22513
ChainResidueDetails
RCYS151
RALA182
RGLY211
RVAL234
GCYS151
GALA182
GGLY211
GVAL234

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Activates thiol group during catalysis => ECO:0000305|PubMed:16239728, ECO:0000305|PubMed:16510976
ChainResidueDetails
RALA179
GALA179

site_idSWS_FT_FI5
Number of Residues10
DetailsMOD_RES: N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946
ChainResidueDetails
RVAL5
GGLU334
RLEU66
RVAL260
RGLU263
RGLU334
GVAL5
GLEU66
GVAL260
GGLU263

site_idSWS_FT_FI6
Number of Residues14
DetailsMOD_RES: Deamidated asparagine => ECO:0000269|PubMed:18183946
ChainResidueDetails
RGLY9
GGLY70
GALA149
GCYS155
GGLY225
GGLU316
RGLY64
RGLY70
RALA149
RCYS155
RGLY225
RGLU316
GGLY9
GGLY64

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
RMET42
GMET42

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Methionine sulfoxide; in vitro => ECO:0000305|PubMed:25086035
ChainResidueDetails
RPHE46
GPHE46

site_idSWS_FT_FI9
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
RALA61
RVAL219
RTYR254
GALA61
GVAL219
GTYR254

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:18183946, ECO:0007744|PubMed:20068231
ChainResidueDetails
RILE75
GILE75

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
RASN83
GASN83

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:18183946
ChainResidueDetails
RALA122
RASN148
GALA122
GASN148

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
RCYS151
GCYS151

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine; in reversibly inhibited form => ECO:0000250|UniProtKB:P04797
ChainResidueDetails
RTHR152
GTHR152

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
RTHR153
GTHR153

site_idSWS_FT_FI16
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
RVAL177
RALA182
GVAL177
GALA182

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
ChainResidueDetails
RGLN184
GGLN184

site_idSWS_FT_FI18
Number of Residues4
DetailsMOD_RES: N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771
ChainResidueDetails
RLEU194
RALA215
GLEU194
GALA215

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
RGLY211
GGLY211

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
RLEU227
GLEU227

site_idSWS_FT_FI21
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:18183946, ECO:0007744|PubMed:23186163
ChainResidueDetails
RGLY229
GGLY229

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:18183946
ChainResidueDetails
RALA237
GALA237

site_idSWS_FT_FI23
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
RVAL241
GVAL241

site_idSWS_FT_FI24
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:22771119, ECO:0000269|PubMed:25417112
ChainResidueDetails
RARG247
GARG247

site_idSWS_FT_FI25
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:18183946, ECO:0007744|PubMed:19690332
ChainResidueDetails
RTRP312
GTRP312

site_idSWS_FT_FI26
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
RLYS333
GLYS333

site_idSWS_FT_FI27
Number of Residues4
DetailsCARBOHYD: (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:28522607
ChainResidueDetails
RGLY197
RGLY200
GGLY197
GGLY200

site_idSWS_FT_FI28
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
RTHR186
GTHR186

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
RCYS151
RHIS178

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
GCYS151
GHIS178

225946

PDB entries from 2024-10-09

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