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3FWN

Dimeric 6-phosphogluconate dehydrogenase complexed with 6-phosphogluconate and 2'-monophosphoadenosine-5'-diphosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004616molecular_functionphosphogluconate dehydrogenase (decarboxylating) activity
A0005829cellular_componentcytosol
A0006098biological_processpentose-phosphate shunt
A0008114molecular_functionphosphogluconate 2-dehydrogenase activity
A0009051biological_processpentose-phosphate shunt, oxidative branch
A0016054biological_processorganic acid catabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019521biological_processD-gluconate metabolic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046177biological_processD-gluconate catabolic process
A0050661molecular_functionNADP binding
A0097216molecular_functionguanosine tetraphosphate binding
B0004616molecular_functionphosphogluconate dehydrogenase (decarboxylating) activity
B0005829cellular_componentcytosol
B0006098biological_processpentose-phosphate shunt
B0008114molecular_functionphosphogluconate 2-dehydrogenase activity
B0009051biological_processpentose-phosphate shunt, oxidative branch
B0016054biological_processorganic acid catabolic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019521biological_processD-gluconate metabolic process
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046177biological_processD-gluconate catabolic process
B0050661molecular_functionNADP binding
B0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 6PG A 2002
ChainResidue
ASER128
ALYS260
AARG287
AILE365
AHOH517
AHOH646
AHOH680
AHOH912
AHOH967
BARG445
BPHE448
AGLY129
BHIS451
AGLY130
ALYS183
AHIS186
AASN187
AGLU190
ATYR191
AASN259

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ATR B 2000
ChainResidue
AASN247
BMET11
BALA12
BASN33
BARG34
BSER35
BLYS38
BVAL74
BLYS75
BGLY79
BLYS260
BHOH673
BHOH949
BHOH1098
BHOH1112
BHOH1113
BHOH1114
BHOH1408
BHOH1424
BHOH1571
BHOH1572
BHOH1669

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 6PG B 2001
ChainResidue
AARG445
APHE448
AHIS451
BASN102
BSER128
BGLY129
BGLY130
BLYS183
BHIS186
BASN187
BGLU190
BTYR191
BASN259
BLYS260
BARG287
BILE365
BHOH638
BHOH692
BHOH867
BHOH1003
BHOH1577

Functional Information from PROSITE/UniProt
site_idPS00461
Number of Residues13
Details6PGD 6-phosphogluconate dehydrogenase signature. IlDeaANKGTGkW
ChainResidueDetails
AILE253-TRP265

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:19686854
ChainResidueDetails
ALYS183
BLYS183

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:19686854
ChainResidueDetails
AGLU190
BGLU190

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AGLY10
BHIS451
AASN33
AVAL74
AARG445
AHIS451
BGLY10
BASN33
BVAL74
BARG445

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: in other chain
ChainResidueDetails
AASN102
ASER128
ALYS260
AARG287
BASN102
BSER128
BLYS260
BARG287

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: in other chain => ECO:0000250
ChainResidueDetails
AHIS186
ATYR191
BHIS186
BTYR191

218853

PDB entries from 2024-04-24

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