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1TXG

Structure of glycerol-3-phosphate dehydrogenase from Archaeoglobus fulgidus

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006072biological_processglycerol-3-phosphate metabolic process
A0006650biological_processglycerophospholipid metabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0046167biological_processglycerol-3-phosphate biosynthetic process
A0046168biological_processglycerol-3-phosphate catabolic process
A0051287molecular_functionNAD binding
A0141153molecular_functionglycerol-3-phosphate dehydrogenase (NADP+) activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006072biological_processglycerol-3-phosphate metabolic process
B0006650biological_processglycerophospholipid metabolic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0046167biological_processglycerol-3-phosphate biosynthetic process
B0046168biological_processglycerol-3-phosphate catabolic process
B0051287molecular_functionNAD binding
B0141153molecular_functionglycerol-3-phosphate dehydrogenase (NADP+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1001
ChainResidue
BARG147
BHOH1175
BHOH1292

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1002
ChainResidue
ALYS53
AASN55
AHOH1070
AHOH1126

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1003
ChainResidue
AASN193
AHOH1078
AHOH1239
ALYS105
ALYS192

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1004
ChainResidue
AARG256
AGLY257
AGLY258
AHOH1052
AHOH1159

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1005
ChainResidue
AARG203
AARG256
AGOL1009
AHOH1067
AHOH1158
AHOH1334

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 1006
ChainResidue
BARG256
BGLY257
BGLY258
BHOH1065
BHOH1197
BHOH1201
BHOH1243

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1007
ChainResidue
BLYS105
BLYS192
BASN193
BHOH1120
BHOH1145
BHOH1280

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1008
ChainResidue
BGLY258
BARG259
BHOH1341

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NH4 B 1011
ChainResidue
BLEU115
BTHR116
BGLU119
BHOH1114
BHOH1381
BHOH1382

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1009
ChainResidue
AALA200
AARG203
ALYS217
APHE255
ASO41005
AHOH1020
AHOH1031
AHOH1112

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 1010
ChainResidue
BALA200
BARG203
BLYS217
BPHE255
BHOH1022
BHOH1059
BHOH1248

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00394
ChainResidueDetails
ALYS192
BLYS192

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A0A0F6AK91
ChainResidueDetails
AGLY137
BALA141
BLYS192
BASP250
BARG259
BASN260
BVAL287
BGLU289
AALA141
ALYS192
AASP250
AARG259
AASN260
AVAL287
AGLU289
BGLY137

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1evy
ChainResidueDetails
ALYS192
ATHR254

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1evy
ChainResidueDetails
BLYS192
BTHR254

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PDB entries from 2024-07-31

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