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1J0X

Crystal structure of the rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH)

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
O0005829cellular_componentcytosol
O0005856cellular_componentcytoskeleton
O0006006biological_processglucose metabolic process
O0006096biological_processglycolytic process
O0006417biological_processregulation of translation
O0006915biological_processapoptotic process
O0008017molecular_functionmicrotubule binding
O0015630cellular_componentmicrotubule cytoskeleton
O0016491molecular_functionoxidoreductase activity
O0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
O0016740molecular_functiontransferase activity
O0032481biological_processpositive regulation of type I interferon production
O0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
O0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
O0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
O0045087biological_processinnate immune response
O0050661molecular_functionNADP binding
O0050821biological_processprotein stabilization
O0051287molecular_functionNAD binding
O0051402biological_processneuron apoptotic process
O0097452cellular_componentGAIT complex
P0000226biological_processmicrotubule cytoskeleton organization
P0002376biological_processimmune system process
P0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
P0005515molecular_functionprotein binding
P0005634cellular_componentnucleus
P0005737cellular_componentcytoplasm
P0005829cellular_componentcytosol
P0005856cellular_componentcytoskeleton
P0006006biological_processglucose metabolic process
P0006096biological_processglycolytic process
P0006417biological_processregulation of translation
P0006915biological_processapoptotic process
P0008017molecular_functionmicrotubule binding
P0015630cellular_componentmicrotubule cytoskeleton
P0016491molecular_functionoxidoreductase activity
P0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
P0016740molecular_functiontransferase activity
P0032481biological_processpositive regulation of type I interferon production
P0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
P0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
P0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
P0045087biological_processinnate immune response
P0050661molecular_functionNADP binding
P0050821biological_processprotein stabilization
P0051287molecular_functionNAD binding
P0051402biological_processneuron apoptotic process
P0097452cellular_componentGAIT complex
Q0000226biological_processmicrotubule cytoskeleton organization
Q0002376biological_processimmune system process
Q0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
Q0005515molecular_functionprotein binding
Q0005634cellular_componentnucleus
Q0005737cellular_componentcytoplasm
Q0005829cellular_componentcytosol
Q0005856cellular_componentcytoskeleton
Q0006006biological_processglucose metabolic process
Q0006096biological_processglycolytic process
Q0006417biological_processregulation of translation
Q0006915biological_processapoptotic process
Q0008017molecular_functionmicrotubule binding
Q0015630cellular_componentmicrotubule cytoskeleton
Q0016491molecular_functionoxidoreductase activity
Q0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Q0016740molecular_functiontransferase activity
Q0032481biological_processpositive regulation of type I interferon production
Q0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
Q0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
Q0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
Q0045087biological_processinnate immune response
Q0050661molecular_functionNADP binding
Q0050821biological_processprotein stabilization
Q0051287molecular_functionNAD binding
Q0051402biological_processneuron apoptotic process
Q0097452cellular_componentGAIT complex
R0000226biological_processmicrotubule cytoskeleton organization
R0002376biological_processimmune system process
R0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
R0005515molecular_functionprotein binding
R0005634cellular_componentnucleus
R0005737cellular_componentcytoplasm
R0005829cellular_componentcytosol
R0005856cellular_componentcytoskeleton
R0006006biological_processglucose metabolic process
R0006096biological_processglycolytic process
R0006417biological_processregulation of translation
R0006915biological_processapoptotic process
R0008017molecular_functionmicrotubule binding
R0015630cellular_componentmicrotubule cytoskeleton
R0016491molecular_functionoxidoreductase activity
R0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
R0016740molecular_functiontransferase activity
R0032481biological_processpositive regulation of type I interferon production
R0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
R0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
R0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
R0045087biological_processinnate immune response
R0050661molecular_functionNADP binding
R0050821biological_processprotein stabilization
R0051287molecular_functionNAD binding
R0051402biological_processneuron apoptotic process
R0097452cellular_componentGAIT complex
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NAD P 1336
ChainResidue
PASN6
PARG77
PSER95
PTHR96
PGLY97
PPHE99
PSER119
PALA120
PCSX149
PASN313
PTYR317
PPHE8
PHOH1375
PGLY9
PARG10
PILE11
PASP32
PPRO33
PPHE34
PILE35

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAD R 2336
ChainResidue
OHOH363
RASN6
RPHE8
RGLY9
RARG10
RILE11
RASP32
RPRO33
RPHE34
RILE35
RARG77
RSER95
RTHR96
RGLY97
RPHE99
RSER119
RALA120
RCSX149
RASN313
RTYR317
RHOH2428

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
OALA147-LEU154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsMotif: {"description":"[IL]-x-C-x-x-[DE] motif","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14646080","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues12
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":"14646080","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues16
DetailsModified residue: {"description":"N6,N6-dimethyllysine","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues28
DetailsModified residue: {"description":"Deamidated asparagine","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues12
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues32
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues20
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"S-nitrosocysteine; in reversibly inhibited form","evidences":[{"source":"UniProtKB","id":"P04797","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues8
DetailsModified residue: {"description":"N6-malonyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues4
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
OHIS176

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
PHIS176

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
QHIS176

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
RHIS176

239803

PDB entries from 2025-08-06

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