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1DPG

GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES

Functional Information from GO Data
ChainGOidnamespacecontents
A0004345molecular_functionglucose-6-phosphate dehydrogenase activity
A0005829cellular_componentcytosol
A0006006biological_processglucose metabolic process
A0006098biological_processpentose-phosphate shunt
A0009051biological_processpentose-phosphate shunt, oxidative branch
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0050661molecular_functionNADP binding
B0004345molecular_functionglucose-6-phosphate dehydrogenase activity
B0005829cellular_componentcytosol
B0006006biological_processglucose metabolic process
B0006098biological_processpentose-phosphate shunt
B0009051biological_processpentose-phosphate shunt, oxidative branch
B0016491molecular_functionoxidoreductase activity
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 2000
ChainResidue
AGLU147
ALYS148
AILE176
AASP177
AHIS178
AHIS240
ATYR415
AHOH2079
AHOH2265

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 2002
ChainResidue
AHIS178
ATYR179
ALYS182
ALYS343
AHOH2291

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 B 2001
ChainResidue
BGLU147
BLYS148
BILE176
BASP177
BHIS178
BHIS240
BTYR415
BHOH2172
BHOH2216

Functional Information from PROSITE/UniProt
site_idPS00069
Number of Residues7
DetailsG6P_DEHYDROGENASE Glucose-6-phosphate dehydrogenase active site. DHYLGKE
ChainResidueDetails
AASP177-GLU183

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:9485426
ChainResidueDetails
ATHR241
BTHR241

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:11320304, ECO:0000269|PubMed:9485426
ChainResidueDetails
AGLY13
AGLN47
AVAL86
BGLY13
BGLN47
BVAL86

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:11320304
ChainResidueDetails
APRO149
BPRO149

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000305|PubMed:11106478
ChainResidueDetails
ATYR179
BMET236
BARG339
BGLN344
AGLU183
AVAL217
AMET236
AARG339
AGLN344
BTYR179
BGLU183
BVAL217

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 7881907
ChainResidueDetails
AASP177
AHIS240

site_idCSA2
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 7881907
ChainResidueDetails
BASP177
BHIS240

site_idMCSA1
Number of Residues3
DetailsM-CSA 843
ChainResidueDetails
AASP177modifies pKa
AHIS178transition state stabiliser
AHIS240proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 843
ChainResidueDetails
BASP177modifies pKa
BHIS178transition state stabiliser
BHIS240proton acceptor, proton donor

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PDB entries from 2025-06-18

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