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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9L3E

Structure of GAPDH complexed with Leu-F

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
O0000226biological_processmicrotubule cytoskeleton organization
O0001819biological_processpositive regulation of cytokine production
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
O0006096biological_processglycolytic process
O0006417biological_processregulation of translation
O0006915biological_processapoptotic process
O0008017molecular_functionmicrotubule binding
O0010951biological_processnegative regulation of endopeptidase activity
O0015630cellular_componentmicrotubule cytoskeleton
O0016020cellular_componentmembrane
O0016241biological_processregulation of macroautophagy
O0016491molecular_functionoxidoreductase activity
O0016740molecular_functiontransferase activity
O0017148biological_processnegative regulation of translation
O0019828molecular_functionaspartic-type endopeptidase inhibitor activity
O0031640biological_processkilling of cells of another organism
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
O0050821biological_processprotein stabilization
O0050832biological_processdefense response to fungus
O0051402biological_processneuron apoptotic process
O0051873biological_processkilling by host of symbiont cells
O0061621biological_processcanonical glycolysis
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
P0001819biological_processpositive regulation of cytokine production
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
P0006096biological_processglycolytic process
P0006417biological_processregulation of translation
P0006915biological_processapoptotic process
P0008017molecular_functionmicrotubule binding
P0010951biological_processnegative regulation of endopeptidase activity
P0015630cellular_componentmicrotubule cytoskeleton
P0016020cellular_componentmembrane
P0016241biological_processregulation of macroautophagy
P0016491molecular_functionoxidoreductase activity
P0016740molecular_functiontransferase activity
P0017148biological_processnegative regulation of translation
P0019828molecular_functionaspartic-type endopeptidase inhibitor activity
P0031640biological_processkilling of cells of another organism
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
P0050821biological_processprotein stabilization
P0050832biological_processdefense response to fungus
P0051402biological_processneuron apoptotic process
P0051873biological_processkilling by host of symbiont cells
P0061621biological_processcanonical glycolysis
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
Q0001819biological_processpositive regulation of cytokine production
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
Q0006096biological_processglycolytic process
Q0006417biological_processregulation of translation
Q0006915biological_processapoptotic process
Q0008017molecular_functionmicrotubule binding
Q0010951biological_processnegative regulation of endopeptidase activity
Q0015630cellular_componentmicrotubule cytoskeleton
Q0016020cellular_componentmembrane
Q0016241biological_processregulation of macroautophagy
Q0016491molecular_functionoxidoreductase activity
Q0016740molecular_functiontransferase activity
Q0017148biological_processnegative regulation of translation
Q0019828molecular_functionaspartic-type endopeptidase inhibitor activity
Q0031640biological_processkilling of cells of another organism
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
Q0050821biological_processprotein stabilization
Q0050832biological_processdefense response to fungus
Q0051402biological_processneuron apoptotic process
Q0051873biological_processkilling by host of symbiont cells
Q0061621biological_processcanonical glycolysis
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
R0001819biological_processpositive regulation of cytokine production
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
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
R0016740molecular_functiontransferase activity
R0017148biological_processnegative regulation of translation
R0019828molecular_functionaspartic-type endopeptidase inhibitor activity
R0031640biological_processkilling of cells of another organism
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
R0050821biological_processprotein stabilization
R0050832biological_processdefense response to fungus
R0051402biological_processneuron apoptotic process
R0051873biological_processkilling by host of symbiont cells
R0061621biological_processcanonical glycolysis
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 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 Residues20
DetailsMotif: {"description":"[IL]-x-C-x-x-[DE] motif","evidences":[{"source":"PubMed","id":"25417112","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"25086035","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16239728","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16510976","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P22513","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
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_FI6
Number of Residues20
DetailsModified residue: {"description":"N6,N6-dimethyllysine","evidences":[{"source":"PubMed","id":"18183946","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues28
DetailsModified residue: {"description":"Deamidated asparagine","evidences":[{"source":"PubMed","id":"18183946","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"Methionine sulfoxide; in vitro","evidences":[{"source":"PubMed","id":"25086035","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues12
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
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_FI12
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_FI13
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18183946","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
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_FI15
Number of Residues4
DetailsModified residue: {"description":"S-nitrosocysteine; in reversibly inhibited form","evidences":[{"source":"UniProtKB","id":"P04797","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues8
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
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_FI19
Number of Residues8
DetailsModified residue: {"description":"N6-malonyllysine; alternate","evidences":[{"source":"PubMed","id":"21908771","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
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_FI23
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18183946","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI25
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_FI26
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_FI27
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues8
DetailsGlycosylation: {"description":"(Microbial infection) N-beta-linked (GlcNAc) arginine","evidences":[{"source":"PubMed","id":"28522607","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI29
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
site_idSWS_FT_FI30
Number of Residues292
DetailsRegion: {"description":"Interaction with WARS1","evidences":[{"source":"PubMed","id":"15628863","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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