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1G6K

Crystal structure of glucose dehydrogenase mutant E96A complexed with NAD+

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0030435biological_processsporulation resulting in formation of a cellular spore
A0047934molecular_functionglucose 1-dehydrogenase (NAD+) activity
A0047935molecular_functionglucose 1-dehydrogenase (NADP+) activity
A0047936molecular_functionglucose 1-dehydrogenase [NAD(P)] activity
B0016491molecular_functionoxidoreductase activity
B0030435biological_processsporulation resulting in formation of a cellular spore
B0047934molecular_functionglucose 1-dehydrogenase (NAD+) activity
B0047935molecular_functionglucose 1-dehydrogenase (NADP+) activity
B0047936molecular_functionglucose 1-dehydrogenase [NAD(P)] activity
E0016491molecular_functionoxidoreductase activity
E0030435biological_processsporulation resulting in formation of a cellular spore
E0047934molecular_functionglucose 1-dehydrogenase (NAD+) activity
E0047935molecular_functionglucose 1-dehydrogenase (NADP+) activity
E0047936molecular_functionglucose 1-dehydrogenase [NAD(P)] activity
F0016491molecular_functionoxidoreductase activity
F0030435biological_processsporulation resulting in formation of a cellular spore
F0047934molecular_functionglucose 1-dehydrogenase (NAD+) activity
F0047935molecular_functionglucose 1-dehydrogenase (NADP+) activity
F0047936molecular_functionglucose 1-dehydrogenase [NAD(P)] activity
Functional Information from PDB Data
site_idAC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NAD A 1262
ChainResidue
AGLY14
AALA93
AGLY94
ATHR115
AMET143
ASER144
ASER145
ATYR158
ALYS162
APRO188
AGLY189
ATHR17
AILE191
ATHR193
AILE195
AASN196
AHOH1273
AHOH1291
AHOH1299
AHOH1300
AGLY18
ALEU19
AARG39
AGLY64
AASP65
AVAL66
AASN92

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE NAD B 2262
ChainResidue
BGLY14
BTHR17
BGLY18
BLEU19
BGLY64
BASP65
BVAL66
BASN92
BALA93
BGLY94
BTHR115
BMET143
BSER144
BSER145
BTYR158
BLYS162
BPRO188
BGLY189
BILE191
BTHR193
BILE195
BASN196
BHOH2265
BHOH2293
BHOH2331

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE NAD E 3262
ChainResidue
EGLY14
ETHR17
EGLY18
ELEU19
EARG39
EGLY64
EASP65
EVAL66
EASN92
EALA93
EGLY94
ETHR115
EMET143
ESER144
ESER145
ETYR158
ELYS162
EPRO188
EGLY189
EILE191
ETHR193
EILE195
EASN196
EHOH3279
EHOH3284

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAD F 4262
ChainResidue
FHOH4272
FHOH4304
FGLY14
FTHR17
FGLY18
FLEU19
FGLY64
FASP65
FVAL66
FASN92
FALA93
FGLY94
FTHR115
FMET143
FSER144
FSER145
FTYR158
FLYS162
FPRO188
FGLY189
FILE191
FTHR193
FILE195
FASN196

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SvhekipwplFvhYAASKGGMkLMTeTLA
ChainResidueDetails
ASER145-ALA173

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ATYR158
BTYR158
ETYR158
FTYR158

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11173533
ChainResidueDetails
AVAL11
BVAL11
EVAL11
FVAL11

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER145
BSER145
ESER145
FSER145

217705

PDB entries from 2024-03-27

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