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

3DMT

Structure of Glycosomal Glyceraldehyde-3-Phosphate Dehydrogenase from Trypanosoma cruzi in complex with the irreversible iodoacetate inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A0005829cellular_componentcytosol
A0006006biological_processglucose metabolic process
A0006096biological_processglycolytic process
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0020015cellular_componentglycosome
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
B0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
B0005829cellular_componentcytosol
B0006006biological_processglucose metabolic process
B0006096biological_processglycolytic process
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0020015cellular_componentglycosome
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
C0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
C0005829cellular_componentcytosol
C0006006biological_processglucose metabolic process
C0006096biological_processglycolytic process
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0020015cellular_componentglycosome
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
D0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
D0005829cellular_componentcytosol
D0006006biological_processglucose metabolic process
D0006096biological_processglycolytic process
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0020015cellular_componentglycosome
D0050661molecular_functionNADP binding
D0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAD C 360
ChainResidue
CASN8
CTHR111
CGLY112
CLEU113
CSER134
CALA135
CALA198
CASN335
CGLU336
CTYR339
CGLY9
CGLY11
CARG12
CILE13
CASP38
CALA90
CGLN91
CSER110

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE NAD D 360
ChainResidue
DGLY9
DGLY11
DARG12
DILE13
DASP38
DMET39
DALA90
DGLN91
DSER110
DTHR111
DGLY112
DLEU113
DSER134
DALA135
DCYS166
DALA198
DASN335
DGLU336
DTYR339

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NAD A 360
ChainResidue
AGLY9
APHE10
AGLY11
AARG12
AILE13
AASP38
AMET39
AALA90
AGLN91
ASER110
ATHR111
AGLY112
ALEU113
ASER134
AALA135
ACYS166
AALA198
AASN335
AGLU336
ATYR339

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE NAD B 360
ChainResidue
BGLY9
BPHE10
BGLY11
BARG12
BILE13
BASP38
BMET39
BALA90
BGLN91
BSER110
BTHR111
BGLY112
BLEU113
BSER134
BALA135
BCYS166
BALA198
BASN335
BTYR339

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL C 361
ChainResidue
CTHR197
CTHR199

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
AALA164-LEU171
CALA164-LEU171

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsMotif: {"description":"Microbody targeting signal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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

site_idSWS_FT_FI3
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12795610","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14622286","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues18
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Activates thiol group during catalysis"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
ACYS166
AHIS194

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
BCYS166
BHIS194

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
DCYS166
DHIS194

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
CHIS194

243531

PDB entries from 2025-10-22

PDB statisticsPDBj update infoContact PDBjnumon