Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6M61

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) with inhibitor heptelidic acid

Functional Information from GO Data
ChainGOidnamespacecontents
O0000226biological_processmicrotubule cytoskeleton organization
O0002376biological_processimmune system process
O0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
O0005515molecular_functionprotein binding
O0005634cellular_componentnucleus
O0005737cellular_componentcytoplasm
O0005811cellular_componentlipid droplet
O0005829cellular_componentcytosol
O0005856cellular_componentcytoskeleton
O0005886cellular_componentplasma membrane
O0006006biological_processglucose metabolic process
O0006096biological_processglycolytic process
O0006417biological_processregulation of translation
O0006915biological_processapoptotic process
O0008017molecular_functionmicrotubule binding
O0015630cellular_componentmicrotubule cytoskeleton
O0016020cellular_componentmembrane
O0016241biological_processregulation of macroautophagy
O0016491molecular_functionoxidoreductase activity
O0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
O0016740molecular_functiontransferase activity
O0017148biological_processnegative regulation of translation
O0019828molecular_functionaspartic-type endopeptidase inhibitor activity
O0031982cellular_componentvesicle
O0032481biological_processpositive regulation of type I interferon production
O0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
O0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
O0042802molecular_functionidentical protein binding
O0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
O0045087biological_processinnate immune response
O0048471cellular_componentperinuclear region of cytoplasm
O0050661molecular_functionNADP binding
O0050821biological_processprotein stabilization
O0051287molecular_functionNAD binding
O0051402biological_processneuron apoptotic process
O0061621biological_processcanonical glycolysis
O0061760biological_processantifungal innate immune response
O0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
O0070062cellular_componentextracellular exosome
O0071346biological_processcellular response to type II interferon
O0097452cellular_componentGAIT complex
O0097718molecular_functiondisordered domain specific binding
O1901194biological_processnegative regulation of formation of translation preinitiation complex
O1990904cellular_componentribonucleoprotein complex
P0000226biological_processmicrotubule cytoskeleton organization
P0002376biological_processimmune system process
P0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
P0005515molecular_functionprotein binding
P0005634cellular_componentnucleus
P0005737cellular_componentcytoplasm
P0005811cellular_componentlipid droplet
P0005829cellular_componentcytosol
P0005856cellular_componentcytoskeleton
P0005886cellular_componentplasma membrane
P0006006biological_processglucose metabolic process
P0006096biological_processglycolytic process
P0006417biological_processregulation of translation
P0006915biological_processapoptotic process
P0008017molecular_functionmicrotubule binding
P0015630cellular_componentmicrotubule cytoskeleton
P0016020cellular_componentmembrane
P0016241biological_processregulation of macroautophagy
P0016491molecular_functionoxidoreductase activity
P0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
P0016740molecular_functiontransferase activity
P0017148biological_processnegative regulation of translation
P0019828molecular_functionaspartic-type endopeptidase inhibitor activity
P0031982cellular_componentvesicle
P0032481biological_processpositive regulation of type I interferon production
P0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
P0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
P0042802molecular_functionidentical protein binding
P0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
P0045087biological_processinnate immune response
P0048471cellular_componentperinuclear region of cytoplasm
P0050661molecular_functionNADP binding
P0050821biological_processprotein stabilization
P0051287molecular_functionNAD binding
P0051402biological_processneuron apoptotic process
P0061621biological_processcanonical glycolysis
P0061760biological_processantifungal innate immune response
P0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
P0070062cellular_componentextracellular exosome
P0071346biological_processcellular response to type II interferon
P0097452cellular_componentGAIT complex
P0097718molecular_functiondisordered domain specific binding
P1901194biological_processnegative regulation of formation of translation preinitiation complex
P1990904cellular_componentribonucleoprotein complex
Q0000226biological_processmicrotubule cytoskeleton organization
Q0002376biological_processimmune system process
Q0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
Q0005515molecular_functionprotein binding
Q0005634cellular_componentnucleus
Q0005737cellular_componentcytoplasm
Q0005811cellular_componentlipid droplet
Q0005829cellular_componentcytosol
Q0005856cellular_componentcytoskeleton
Q0005886cellular_componentplasma membrane
Q0006006biological_processglucose metabolic process
Q0006096biological_processglycolytic process
Q0006417biological_processregulation of translation
Q0006915biological_processapoptotic process
Q0008017molecular_functionmicrotubule binding
Q0015630cellular_componentmicrotubule cytoskeleton
Q0016020cellular_componentmembrane
Q0016241biological_processregulation of macroautophagy
Q0016491molecular_functionoxidoreductase activity
Q0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Q0016740molecular_functiontransferase activity
Q0017148biological_processnegative regulation of translation
Q0019828molecular_functionaspartic-type endopeptidase inhibitor activity
Q0031982cellular_componentvesicle
Q0032481biological_processpositive regulation of type I interferon production
Q0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
Q0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
Q0042802molecular_functionidentical protein binding
Q0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
Q0045087biological_processinnate immune response
Q0048471cellular_componentperinuclear region of cytoplasm
Q0050661molecular_functionNADP binding
Q0050821biological_processprotein stabilization
Q0051287molecular_functionNAD binding
Q0051402biological_processneuron apoptotic process
Q0061621biological_processcanonical glycolysis
Q0061760biological_processantifungal innate immune response
Q0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
Q0070062cellular_componentextracellular exosome
Q0071346biological_processcellular response to type II interferon
Q0097452cellular_componentGAIT complex
Q0097718molecular_functiondisordered domain specific binding
Q1901194biological_processnegative regulation of formation of translation preinitiation complex
Q1990904cellular_componentribonucleoprotein complex
R0000226biological_processmicrotubule cytoskeleton organization
R0002376biological_processimmune system process
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
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
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
R0045087biological_processinnate immune response
R0048471cellular_componentperinuclear region of cytoplasm
R0050661molecular_functionNADP binding
R0050821biological_processprotein stabilization
R0051287molecular_functionNAD binding
R0051402biological_processneuron apoptotic process
R0061621biological_processcanonical glycolysis
R0061760biological_processantifungal innate immune response
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
R1901194biological_processnegative regulation of formation of translation preinitiation complex
R1990904cellular_componentribonucleoprotein complex
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue EDO O 401
ChainResidue
OLYS162
OVAL163
OASP166
OASN167
OHOH543
OHOH608

site_idAC2
Number of Residues4
Detailsbinding site for residue EDO O 402
ChainResidue
OHOH655
OASP39
OLEU40
OASN41

site_idAC3
Number of Residues4
Detailsbinding site for residue PEG O 403
ChainResidue
OPRO129
OMET130
OPHE131
OHOH582

site_idAC4
Number of Residues3
Detailsbinding site for residue ZN O 404
ChainResidue
OHIS57
OHOH559
OHOH783

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN O 405
ChainResidue
OASP289
OHIS291
OHOH598
OHOH741

site_idAC6
Number of Residues13
Detailsbinding site for residue F4F O 406
ChainResidue
OPRO124
OSER151
OCYS152
OTHR153
OHIS179
OTHR211
OGLY212
OARG234
ONAD407
OHOH508
OHOH509
OHOH535
OHOH563

site_idAC7
Number of Residues33
Detailsbinding site for residue NAD O 407
ChainResidue
OASN9
OGLY10
OPHE11
OGLY12
OARG13
OILE14
OASN34
OASP35
OPRO36
OPHE37
OARG80
OSER98
OTHR99
OGLY100
OSER122
OALA123
OCYS152
OALA183
OASN316
OTYR320
OF4F406
OHOH530
OHOH538
OHOH558
OHOH569
OHOH591
OHOH595
OHOH597
OHOH599
OHOH616
OHOH657
OHOH664
OHOH674

site_idAC8
Number of Residues3
Detailsbinding site for residue EDO Q 401
ChainResidue
QPRO129
QMET130
QASN136

site_idAC9
Number of Residues5
Detailsbinding site for residue EDO Q 402
ChainResidue
OHOH770
QGLY88
QASP89
QGLY115
QHOH668

site_idAD1
Number of Residues5
Detailsbinding site for residue EDO Q 403
ChainResidue
QASP39
QLEU40
QILE76
QGLN78
QHOH643

site_idAD2
Number of Residues6
Detailsbinding site for residue EDO Q 404
ChainResidue
OTYR49
QTHR277
QHIS279
QHOH588
QHOH607
QHOH628

site_idAD3
Number of Residues4
Detailsbinding site for residue EDO Q 405
ChainResidue
PGLU106
QPRO252
QLYS254
QASP305

site_idAD4
Number of Residues5
Detailsbinding site for residue ZN Q 406
ChainResidue
QASP289
QHIS291
QHOH588
QHOH651
QHOH735

site_idAD5
Number of Residues30
Detailsbinding site for residue NAD Q 408
ChainResidue
QARG13
QILE14
QASN34
QASP35
QPRO36
QPHE37
QARG80
QSER98
QTHR99
QGLY100
QSER122
QALA123
QCYS152
QALA183
QASN316
QTYR320
QF4F407
QHOH509
QHOH525
QHOH558
QHOH567
QHOH584
QHOH659
QHOH677
QHOH696
QHOH702
QASN9
QGLY10
QPHE11
QGLY12

site_idAD6
Number of Residues4
Detailsbinding site for residue EDO P 401
ChainResidue
PTHR277
PHIS279
PPHE286
PHOH586

site_idAD7
Number of Residues5
Detailsbinding site for residue EDO P 402
ChainResidue
PARG20
PASN24
PPHE56
PHIS57
PPHE318

site_idAD8
Number of Residues3
Detailsbinding site for residue EDO P 403
ChainResidue
PLYS254
PASN304
PASP305

site_idAD9
Number of Residues6
Detailsbinding site for residue ZN P 404
ChainResidue
OHIS330
OHOH528
OHOH549
PGLU335
PHOH624
PHOH666

site_idAE1
Number of Residues5
Detailsbinding site for residue ZN P 405
ChainResidue
PASP289
PHIS291
PHOH586
PHOH664
PHOH721

site_idAE2
Number of Residues5
Detailsbinding site for residue EDO R 401
ChainResidue
RGLY300
RILE301
RALA302
RHOH502
RHOH605

site_idAE3
Number of Residues5
Detailsbinding site for residue GOL R 402
ChainResidue
RGLY193
RLYS194
RTRP196
RHOH535
RHOH606

site_idAE4
Number of Residues17
Detailsbinding site for Di-peptide F4F Q 407 and CYS Q 152
ChainResidue
QPRO124
QSER151
QTHR153
QTHR154
QASN155
QCYS156
QTHR177
QHIS179
QTHR211
QGLY212
QALA213
QARG234
QTYR314
QTYR320
QNAD408
QHOH530
QHOH623

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
OALA150-LEU157

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues438
DetailsRegion: {"description":"Interaction with WARS1","evidences":[{"source":"PubMed","id":"15628863","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsMotif: {"description":"[IL]-x-C-x-x-[DE] motif","evidences":[{"source":"PubMed","id":"25417112","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"25086035","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16239728","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16510976","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P22513","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Activates thiol group during catalysis","evidences":[{"source":"PubMed","id":"16239728","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16510976","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues19
DetailsModified residue: {"description":"N6,N6-dimethyllysine","evidences":[{"source":"PubMed","id":"18183946","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues28
DetailsModified residue: {"description":"Deamidated asparagine","evidences":[{"source":"PubMed","id":"18183946","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"Methionine sulfoxide; in vitro","evidences":[{"source":"PubMed","id":"25086035","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues12
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18183946","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18183946","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues4
DetailsModified residue: {"description":"S-nitrosocysteine; in reversibly inhibited form","evidences":[{"source":"UniProtKB","id":"P04797","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues8
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues8
DetailsModified residue: {"description":"N6-malonyllysine; alternate","evidences":[{"source":"PubMed","id":"21908771","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18183946","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18183946","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues4
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"22771119","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25417112","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18183946","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues8
DetailsGlycosylation: {"description":"(Microbial infection) N-beta-linked (GlcNAc) arginine","evidences":[{"source":"PubMed","id":"28522607","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI30
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon