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4WNI

Crystal structure of the T229K mutant of human GAPDH at 2.3 angstroems resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000226biological_processmicrotubule cytoskeleton organization
A0001819biological_processpositive regulation of cytokine production
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
A0010951biological_processnegative regulation of endopeptidase activity
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
A0031640biological_processkilling of cells of another organism
A0031965cellular_componentnuclear membrane
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
A0050832biological_processdefense response to fungus
A0051287molecular_functionNAD binding
A0051402biological_processneuron apoptotic process
A0051873biological_processkilling by host of symbiont cells
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
A1990904cellular_componentribonucleoprotein complex
B0000226biological_processmicrotubule cytoskeleton organization
B0001819biological_processpositive regulation of cytokine production
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
B0010951biological_processnegative regulation of endopeptidase activity
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
B0031640biological_processkilling of cells of another organism
B0031965cellular_componentnuclear membrane
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
B0050832biological_processdefense response to fungus
B0051287molecular_functionNAD binding
B0051402biological_processneuron apoptotic process
B0051873biological_processkilling by host of symbiont cells
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
B1990904cellular_componentribonucleoprotein complex
C0000226biological_processmicrotubule cytoskeleton organization
C0001819biological_processpositive regulation of cytokine production
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
C0010951biological_processnegative regulation of endopeptidase activity
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
C0031640biological_processkilling of cells of another organism
C0031965cellular_componentnuclear membrane
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
C0050832biological_processdefense response to fungus
C0051287molecular_functionNAD binding
C0051402biological_processneuron apoptotic process
C0051873biological_processkilling by host of symbiont cells
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
C1990904cellular_componentribonucleoprotein complex
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
O0006006biological_processglucose metabolic process
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
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
O0031640biological_processkilling of cells of another organism
O0031965cellular_componentnuclear membrane
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
O0050832biological_processdefense response to fungus
O0051287molecular_functionNAD binding
O0051402biological_processneuron apoptotic process
O0051873biological_processkilling by host of symbiont cells
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
O1990904cellular_componentribonucleoprotein complex
Functional Information from PDB Data
site_idAC1
Number of Residues28
Detailsbinding site for residue NAD O 401
ChainResidue
OASN9
OARG80
OSER98
OTHR99
OGLY100
OPHE102
OSER122
OALA123
OCYS152
OALA183
OASN316
OGLY10
OTYR320
OHOH543
OHOH553
OHOH568
OHOH569
OHOH629
OHOH676
OHOH678
OHOH729
OGLY12
OARG13
OILE14
OASN34
OASP35
OPRO36
OPHE37

site_idAC2
Number of Residues6
Detailsbinding site for residue ZN O 402
ChainResidue
BGLU335
BHOH501
BHOH505
OHIS330
OHOH504
OHOH509

site_idAC3
Number of Residues3
Detailsbinding site for residue ZN O 403
ChainResidue
AGLU138
AHIS330
OGLU63

site_idAC4
Number of Residues27
Detailsbinding site for residue NAD A 401
ChainResidue
AASN9
AGLY10
AGLY12
AARG13
AILE14
AASN34
AASP35
APRO36
APHE37
AARG80
ASER98
ATHR99
AGLY100
APHE102
ASER122
AALA123
ACYS152
AALA183
AASN316
AHOH542
AHOH544
AHOH545
AHOH552
AHOH637
AHOH695
AHOH732
AHOH733

site_idAC5
Number of Residues24
Detailsbinding site for residue NAD B 401
ChainResidue
BASN9
BGLY10
BPHE11
BGLY12
BARG13
BILE14
BASN34
BASP35
BPRO36
BPHE37
BARG80
BSER98
BTHR99
BGLY100
BPHE102
BSER122
BALA123
BCYS152
BASN316
BHOH540
BHOH571
BHOH629
BHOH643
BHOH644

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN B 402
ChainResidue
AHIS306
AHOH518
BGLU106
BASP127

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

239149

PDB entries from 2025-07-23

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