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3AY6

Crystal structure of Bacillus megaterium glucose dehydrogenase 4 A258F mutant in complex with NADH and D-glucose

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
C0016491molecular_functionoxidoreductase activity
C0042802molecular_functionidentical protein binding
C0047934molecular_functionglucose 1-dehydrogenase (NAD+) activity
C0047935molecular_functionglucose 1-dehydrogenase (NADP+) activity
C0047936molecular_functionglucose 1-dehydrogenase [NAD(P)+] activity
D0016491molecular_functionoxidoreductase activity
D0042802molecular_functionidentical protein binding
D0047934molecular_functionglucose 1-dehydrogenase (NAD+) activity
D0047935molecular_functionglucose 1-dehydrogenase (NADP+) activity
D0047936molecular_functionglucose 1-dehydrogenase [NAD(P)+] activity
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 Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001
ChainResidueDetails
ATYR158
BTYR158
CTYR158
DTYR158

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AVAL11
ASER145
BVAL11
BSER145
CVAL11
CSER145
DVAL11
DSER145

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PDB entries from 2024-07-24

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