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1IHY

GAPDH complexed with ADP-ribose

Functional Information from GO Data
ChainGOidnamespacecontents
A0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A0005737cellular_componentcytoplasm
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
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
B0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
B0005737cellular_componentcytoplasm
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
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
C0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
C0005737cellular_componentcytoplasm
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
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
D0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
D0005737cellular_componentcytoplasm
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
D0050661molecular_functionNADP binding
D0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
ASER148
ATHR208
AALA210

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 502
ChainResidue
BSER148
BTHR208
BALA210

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 D 503
ChainResidue
DGLY209
DALA210
DHOH526
DSER148
DTHR150
DTHR208

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 504
ChainResidue
CSER148
CTHR208
CGLY209
CALA210

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 505
ChainResidue
ATHR181
AARG231
AAPR335

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 506
ChainResidue
BTHR179
BTHR181
BARG231
BAPR336

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 507
ChainResidue
DTHR179
DTHR181
DARG231
DAPR337
DHOH510

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 508
ChainResidue
CTHR179
CTHR181
CARG231
CAPR338

site_idAC9
Number of Residues16
DetailsBINDING SITE FOR RESIDUE APR A 335
ChainResidue
AASN6
APHE8
AGLY9
AARG10
AILE11
AASP32
APRO33
APHE34
AILE35
AMET77
ASER95
ATHR96
APHE99
ATHR179
AALA180
ASO4505

site_idBC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE APR B 336
ChainResidue
BASN6
BPHE8
BGLY9
BARG10
BILE11
BASP32
BPRO33
BPHE34
BILE35
BMET77
BSER95
BTHR96
BPHE99
BTHR179
BALA180
BSO4506

site_idBC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE APR D 337
ChainResidue
DASN6
DGLY9
DARG10
DILE11
DASP32
DPRO33
DPHE34
DILE35
DMET77
DSER95
DTHR96
DPHE99
DTHR179
DALA180
DSO4507
DHOH513

site_idBC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE APR C 338
ChainResidue
AVAL185
CASN6
CGLY9
CARG10
CILE11
CASP32
CPRO33
CPHE34
CILE35
CMET77
CSER95
CTHR96
CPHE99
CTHR179
CALA180
CSO4508
CHOH511
CHOH524

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
AALA147-LEU154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ACYS149
BCYS149
CCYS149
DCYS149

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:9761850
ChainResidueDetails
AARG10
DARG10
DASP32
DASN313
AASP32
AASN313
BARG10
BASP32
BASN313
CARG10
CASP32
CASN313

site_idSWS_FT_FI3
Number of Residues20
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AMET77
BARG231
CMET77
CSER148
CTHR179
CTHR208
CARG231
DMET77
DSER148
DTHR179
DTHR208
ASER148
DARG231
ATHR179
ATHR208
AARG231
BMET77
BSER148
BTHR179
BTHR208

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Activates thiol group during catalysis
ChainResidueDetails
AHIS176
BHIS176
CHIS176
DHIS176

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P00357
ChainResidueDetails
ASER1
BSER1
CSER1
DSER1

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
ACYS149
AHIS176

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
BCYS149
BHIS176

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
CCYS149
CHIS176

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
DCYS149
DHIS176

site_idMCSA1
Number of Residues2
DetailsM-CSA 911
ChainResidueDetails
ACYS149covalent catalysis, proton shuttle (general acid/base)
AHIS176proton shuttle (general acid/base)

site_idMCSA2
Number of Residues2
DetailsM-CSA 911
ChainResidueDetails
BCYS149covalent catalysis, proton shuttle (general acid/base)
BHIS176proton shuttle (general acid/base)

site_idMCSA3
Number of Residues2
DetailsM-CSA 911
ChainResidueDetails
CCYS149covalent catalysis, proton shuttle (general acid/base)
CHIS176proton shuttle (general acid/base)

site_idMCSA4
Number of Residues2
DetailsM-CSA 911
ChainResidueDetails
DCYS149covalent catalysis, proton shuttle (general acid/base)
DHIS176proton shuttle (general acid/base)

223166

PDB entries from 2024-07-31

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