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1GCO

CRYSTAL STRUCTURE OF GLUCOSE DEHYDROGENASE 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 601
ChainResidue
AGLY14
AGLY94
ATHR115
AMET143
ASER144
ASER145
ATYR158
ALYS162
APRO188
AGLY189
AILE191
ATHR17
ATHR193
APRO194
AILE195
AASN196
AHOH602
AHOH632
AHOH638
AHOH650
AGLY18
ALEU19
AGLY64
AASP65
AVAL66
AASN92
AALA93

site_idAC2
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NAD B 701
ChainResidue
BGLY14
BTHR17
BGLY18
BLEU19
BARG39
BGLY64
BASP65
BVAL66
BASN92
BALA93
BGLY94
BTHR115
BMET143
BSER144
BSER145
BTYR158
BLYS162
BPRO188
BGLY189
BILE191
BTHR193
BPRO194
BILE195
BASN196
BHOH708
BHOH714
BHOH734
BHOH767
BHOH770
BHOH809
BHOH810

site_idAC3
Number of Residues30
DetailsBINDING SITE FOR RESIDUE NAD E 801
ChainResidue
EGLY14
ETHR17
EGLY18
ELEU19
EARG39
EGLY64
EASP65
EVAL66
EASN92
EALA93
EGLY94
ETHR115
EMET143
ESER144
ESER145
ETYR158
ELYS162
EPRO188
EGLY189
EILE191
ETHR193
EPRO194
EILE195
EASN196
EHOH802
EHOH815
EHOH829
EHOH841
EHOH879
EHOH882

site_idAC4
Number of Residues32
DetailsBINDING SITE FOR RESIDUE NAD F 901
ChainResidue
FMET143
FSER144
FSER145
FTYR158
FLYS162
FPRO188
FGLY189
FILE191
FTHR193
FPRO194
FILE195
FASN196
FHOH902
FHOH916
FHOH922
FHOH959
FHOH965
FHOH967
FHOH973
FHOH1010
FHOH1040
FGLY14
FTHR17
FGLY18
FLEU19
FGLY64
FASP65
FVAL66
FASN92
FALA93
FGLY94
FTHR115

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

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PDB entries from 2024-03-27

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