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2VYV

Structure of E.Coli GAPDH Rat Sperm GAPDH heterotetramer

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006006biological_processglucose metabolic process
A0006096biological_processglycolytic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0042802molecular_functionidentical protein binding
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
B0000166molecular_functionnucleotide binding
B0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006006biological_processglucose metabolic process
B0006096biological_processglycolytic process
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0042802molecular_functionidentical protein binding
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
C0000166molecular_functionnucleotide binding
C0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006006biological_processglucose metabolic process
C0006096biological_processglycolytic process
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0042802molecular_functionidentical protein binding
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
D0006006biological_processglucose metabolic process
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 Residues7
DetailsBINDING SITE FOR RESIDUE 1GP D1334
ChainResidue
DCSD149
DHIS176
DTHR179
DTHR181
DARG231
DNAD1340
DHOH2210

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A1330
ChainResidue
ALYS215
AHOH2208
AMET127
AASN133

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT C1330
ChainResidue
CPRO126
CMET127
CHOH2183

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT D1335
ChainResidue
DMET126
DHOH2211
DHOH2212

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT B1330
ChainResidue
BPRO126
BMET127
BLYS215
BHOH2197

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT D1336
ChainResidue
CGLU285
CHOH2148
DARG51

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT B1331
ChainResidue
AARG51
BASN283
BGLU285

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FMT D1337
ChainResidue
DPRO120
DSER148
DTHR151
DGLY209
DALA210
DALA213
DHOH2213
DHOH2214
DHOH2215

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT D1338
ChainResidue
DGLY130
DGLU133
DPRO266

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A1331
ChainResidue
AARG51
BTHR273
BGLU285

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT B1332
ChainResidue
BTHR273
BGLU274

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A1332
ChainResidue
AGLY131
AALA132
APHE134
AHOH2209
AHOH2210

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT B1333
ChainResidue
BGLY131
BPHE134
BASP135
BHOH2069

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT D1339
ChainResidue
DARG17
DHOH2216

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT C1331
ChainResidue
CGLY131
CALA132
CASN133
CPHE134

site_idBC7
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAD A1333
ChainResidue
AGLY7
APHE8
AGLY9
AARG10
AILE11
AASN31
AASP32
AARG76
AALA94
ATHR95
AGLY96
ALEU97
ATHR118
ACSD148
AALA179
AASN312
AHOH2097
AHOH2211
AHOH2213
AHOH2214
AHOH2216
AHOH2217
AHOH2218
AHOH2219

site_idBC8
Number of Residues29
DetailsBINDING SITE FOR RESIDUE NAD B1334
ChainResidue
BGLU313
BTYR316
BHOH2049
BHOH2187
BHOH2198
BHOH2200
BHOH2202
BHOH2203
BHOH2204
BHOH2205
BHOH2206
BHOH2207
CPRO187
BASN6
BGLY9
BARG10
BILE11
BASN31
BASP32
BLEU33
BARG76
BALA94
BTHR95
BGLY96
BLEU97
BTHR118
BCSD148
BALA179
BASN312

site_idBC9
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NAD C1332
ChainResidue
CGLY7
CPHE8
CGLY9
CARG10
CILE11
CASN31
CASP32
CARG76
CALA94
CTHR95
CGLY96
CLEU97
CTHR118
CCSD148
CALA179
CASN312
CTYR316
CHOH2003
CHOH2050
CHOH2057
CHOH2075
CHOH2087
CHOH2185
CHOH2186
CHOH2187
CHOH2188
CHOH2189
CHOH2190

site_idCC1
Number of Residues32
DetailsBINDING SITE FOR RESIDUE NAD D1340
ChainResidue
AHOH2117
DASN6
DGLY7
DPHE8
DGLY9
DARG10
DILE11
DASN30
DASP31
DPRO32
DPHE33
DLYS76
DALA94
DTHR95
DGLY96
DTYR98
DTHR118
DALA119
DCSD149
DALA180
DASN313
DTYR317
D1GP1334
DHOH2063
DHOH2115
DHOH2210
DHOH2217
DHOH2218
DHOH2219
DHOH2220
DHOH2221
DHOH2222

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
AALA146-LEU153
DALA147-LEU154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10009
ChainResidueDetails
DCSD149
BCSD148
CCSD148

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
DARG10
DASN313
DASP31
DLYS76
DTYR98
DTHR118
DSER148
DTHR179
DTHR208
DARG231

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Activates thiol group during catalysis => ECO:0000250
ChainResidueDetails
DHIS176
AASN312
BASP32
BASN312
CASP32
CASN312

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
DSER251
BARG76
CARG76

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:19542219
ChainResidueDetails
ATHR118
BTHR118
CTHR118

site_idSWS_FT_FI6
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:10978154
ChainResidueDetails
ASER147
ATHR207
BSER147
BTHR207
CSER147
CTHR207

site_idSWS_FT_FI7
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00362
ChainResidueDetails
ATHR178
BTHR178
CTHR178

site_idSWS_FT_FI8
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:19542219, ECO:0000269|Ref.18, ECO:0000305|PubMed:10978154
ChainResidueDetails
AARG230
BARG230
CARG230

site_idSWS_FT_FI9
Number of Residues3
DetailsSITE: Activates thiol group during catalysis => ECO:0000269|PubMed:2659073
ChainResidueDetails
AHIS175
BHIS175
CHIS175

site_idSWS_FT_FI10
Number of Residues24
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122
ChainResidueDetails
ALYS113
BLYS122
BLYS211
BLYS215
BLYS223
BLYS247
BLYS255
BLYS259
CLYS113
CLYS122
CLYS211
ALYS122
CLYS215
CLYS223
CLYS247
CLYS255
CLYS259
ALYS211
ALYS215
ALYS223
ALYS247
ALYS255
ALYS259
BLYS113

site_idSWS_FT_FI11
Number of Residues9
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122
ChainResidueDetails
ALYS130
ALYS190
ALYS329
BLYS130
BLYS190
BLYS329
CLYS130
CLYS190
CLYS329

site_idSWS_FT_FI12
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS136
BLYS136
CLYS136

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
DHIS176

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
AHIS175

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
BHIS175

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
CHIS175

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PDB entries from 2024-11-06

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