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3AUT

Crystal structure of Bacillus megaterium glucose dehydrogenase 4 in complex with NADH

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0042802molecular_functionidentical protein binding
A0047934molecular_functionglucose 1-dehydrogenase (NAD+) activity
A0047935molecular_functionglucose 1-dehydrogenase (NADP+) activity
A0047936molecular_functionglucose 1-dehydrogenase [NAD(P)+] activity
B0016491molecular_functionoxidoreductase activity
B0042802molecular_functionidentical protein binding
B0047934molecular_functionglucose 1-dehydrogenase (NAD+) activity
B0047935molecular_functionglucose 1-dehydrogenase (NADP+) activity
B0047936molecular_functionglucose 1-dehydrogenase [NAD(P)+] activity
Functional Information from PDB Data
site_idAC1
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NAI B 301
ChainResidue
BTHR17
BGLY94
BVAL95
BTHR115
BMET143
BSER144
BSER145
BTYR158
BLYS162
BPRO188
BGLY189
BGLY18
BMET191
BTHR193
BPRO194
BILE195
BASN196
BHOH420
BHOH441
BHOH463
BHOH488
BLEU19
BTYR39
BGLY64
BASP65
BVAL66
BASN92
BALA93

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001
ChainResidueDetails
ATYR158
BTYR158

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AVAL11
ASER145
BVAL11
BSER145

226707

PDB entries from 2024-10-30

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