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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6ADE

Crystal structure of phosphorylated mutant of glyceraldehyde 3-phosphate dehydrogenase from human placenta at 3.15A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000226biological_processmicrotubule cytoskeleton organization
A0002376biological_processimmune system process
A0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005811cellular_componentlipid droplet
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0006006biological_processglucose metabolic process
A0006096biological_processglycolytic process
A0006417biological_processregulation of translation
A0006915biological_processapoptotic process
A0008017molecular_functionmicrotubule binding
A0015630cellular_componentmicrotubule cytoskeleton
A0016020cellular_componentmembrane
A0016241biological_processregulation of macroautophagy
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0016740molecular_functiontransferase activity
A0017148biological_processnegative regulation of translation
A0019828molecular_functionaspartic-type endopeptidase inhibitor activity
A0031982cellular_componentvesicle
A0032481biological_processpositive regulation of type I interferon production
A0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
A0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
A0042802molecular_functionidentical protein binding
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0045087biological_processinnate immune response
A0048471cellular_componentperinuclear region of cytoplasm
A0050661molecular_functionNADP binding
A0050821biological_processprotein stabilization
A0051287molecular_functionNAD binding
A0051402biological_processneuron apoptotic process
A0061621biological_processcanonical glycolysis
A0061760biological_processantifungal innate immune response
A0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
A0070062cellular_componentextracellular exosome
A0071346biological_processcellular response to type II interferon
A0097452cellular_componentGAIT complex
A0097718molecular_functiondisordered domain specific binding
A1901194biological_processnegative regulation of formation of translation preinitiation complex
A1990904cellular_componentribonucleoprotein complex
B0000226biological_processmicrotubule cytoskeleton organization
B0002376biological_processimmune system process
B0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005811cellular_componentlipid droplet
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005886cellular_componentplasma membrane
B0006006biological_processglucose metabolic process
B0006096biological_processglycolytic process
B0006417biological_processregulation of translation
B0006915biological_processapoptotic process
B0008017molecular_functionmicrotubule binding
B0015630cellular_componentmicrotubule cytoskeleton
B0016020cellular_componentmembrane
B0016241biological_processregulation of macroautophagy
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0016740molecular_functiontransferase activity
B0017148biological_processnegative regulation of translation
B0019828molecular_functionaspartic-type endopeptidase inhibitor activity
B0031982cellular_componentvesicle
B0032481biological_processpositive regulation of type I interferon production
B0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
B0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
B0042802molecular_functionidentical protein binding
B0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
B0045087biological_processinnate immune response
B0048471cellular_componentperinuclear region of cytoplasm
B0050661molecular_functionNADP binding
B0050821biological_processprotein stabilization
B0051287molecular_functionNAD binding
B0051402biological_processneuron apoptotic process
B0061621biological_processcanonical glycolysis
B0061760biological_processantifungal innate immune response
B0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
B0070062cellular_componentextracellular exosome
B0071346biological_processcellular response to type II interferon
B0097452cellular_componentGAIT complex
B0097718molecular_functiondisordered domain specific binding
B1901194biological_processnegative regulation of formation of translation preinitiation complex
B1990904cellular_componentribonucleoprotein complex
C0000226biological_processmicrotubule cytoskeleton organization
C0002376biological_processimmune system process
C0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005811cellular_componentlipid droplet
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0005886cellular_componentplasma membrane
C0006006biological_processglucose metabolic process
C0006096biological_processglycolytic process
C0006417biological_processregulation of translation
C0006915biological_processapoptotic process
C0008017molecular_functionmicrotubule binding
C0015630cellular_componentmicrotubule cytoskeleton
C0016020cellular_componentmembrane
C0016241biological_processregulation of macroautophagy
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0016740molecular_functiontransferase activity
C0017148biological_processnegative regulation of translation
C0019828molecular_functionaspartic-type endopeptidase inhibitor activity
C0031982cellular_componentvesicle
C0032481biological_processpositive regulation of type I interferon production
C0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
C0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
C0042802molecular_functionidentical protein binding
C0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
C0045087biological_processinnate immune response
C0048471cellular_componentperinuclear region of cytoplasm
C0050661molecular_functionNADP binding
C0050821biological_processprotein stabilization
C0051287molecular_functionNAD binding
C0051402biological_processneuron apoptotic process
C0061621biological_processcanonical glycolysis
C0061760biological_processantifungal innate immune response
C0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
C0070062cellular_componentextracellular exosome
C0071346biological_processcellular response to type II interferon
C0097452cellular_componentGAIT complex
C0097718molecular_functiondisordered domain specific binding
C1901194biological_processnegative regulation of formation of translation preinitiation complex
C1990904cellular_componentribonucleoprotein complex
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue NAD A 401
ChainResidue
AASN9
APHE37
AILE38
AARG80
ASER98
ATHR99
AGLY100
APHE102
ASER122
ACYS152
ATHR182
AGLY10
AASP189
APRO191
AASN316
ATYR320
APHE11
AGLY12
AARG13
AILE14
AASN34
AASP35
APRO36
Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
AALA150-LEU157
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsMotif: {"description":"[IL]-x-C-x-x-[DE] motif","evidences":[{"source":"PubMed","id":"25417112","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"25086035","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16239728","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16510976","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P22513","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues3
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_FI6
Number of Residues12
DetailsModified residue: {"description":"N6,N6-dimethyllysine","evidences":[{"source":"PubMed","id":"18183946","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues21
DetailsModified residue: {"description":"Deamidated asparagine","evidences":[{"source":"PubMed","id":"18183946","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues3
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues3
DetailsModified residue: {"description":"Methionine sulfoxide; in vitro","evidences":[{"source":"PubMed","id":"25086035","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues9
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18183946","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues3
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_FI13
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18183946","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues3
DetailsModified residue: {"description":"S-nitrosocysteine; in reversibly inhibited form","evidences":[{"source":"UniProtKB","id":"P04797","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues6
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues3
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_FI19
Number of Residues6
DetailsModified residue: {"description":"N6-malonyllysine; alternate","evidences":[{"source":"PubMed","id":"21908771","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18183946","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18183946","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues3
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"22771119","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25417112","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18183946","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues6
DetailsGlycosylation: {"description":"(Microbial infection) N-beta-linked (GlcNAc) arginine","evidences":[{"source":"PubMed","id":"28522607","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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