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1CQ1

Soluble Quinoprotein Glucose Dehydrogenase from Acinetobacter Calcoaceticus in Complex with PQQH2 and Glucose

Functional Information from GO Data
ChainGOidnamespacecontents
A0008876molecular_functionquinoprotein glucose dehydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0008876molecular_functionquinoprotein glucose dehydrogenase activity
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS144
BHIS144

site_idSWS_FT_FI2
Number of Residues30
DetailsBINDING: BINDING => ECO:0000269|PubMed:10508152
ChainResidueDetails
AGLN76
ATYR271
AASP273
AGLU309
ATYR343
ATHR348
ALYS377
BGLN76
BASP143
BGLN168
BARG228
AASP143
BGLY247
BPRO248
BGLU253
BTYR263
BALA269
BTYR271
BASP273
BGLU309
BTYR343
BTHR348
AGLN168
BLYS377
AARG228
AGLY247
APRO248
AGLU253
ATYR263
AALA269

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1c9u
ChainResidueDetails
AHIS144
AASP163

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1c9u
ChainResidueDetails
BHIS144
BASP163

site_idMCSA1
Number of Residues7
DetailsM-CSA 104
ChainResidueDetails
AHIS144hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AASP163activator, electrostatic stabiliser, hydrogen bond acceptor
AARG228electrostatic stabiliser, hydrogen bond donor
AALA269metal ligand
ATYR271metal ligand
AASP273metal ligand
AGLU309metal ligand

site_idMCSA2
Number of Residues7
DetailsM-CSA 104
ChainResidueDetails
BHIS144hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BASP163activator, electrostatic stabiliser, hydrogen bond acceptor
BARG228electrostatic stabiliser, hydrogen bond donor
BALA269metal ligand
BTYR271metal ligand
BASP273metal ligand
BGLU309metal ligand

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PDB entries from 2024-07-17

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