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1CRU

SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CALCOACETICUS IN COMPLEX WITH PQQ AND METHYLHYDRAZINE

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 PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 501
ChainResidue
AALA269
ATYR271
AASP273
AGLU309
AHOH632
AHOH663

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 502
ChainResidue
AHOH605
AHOH640
AHOH650
AGLU253
ATYR263
AHOH601

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 503
ChainResidue
AGLY247
APRO248
APQQ504
AHOH615
AHOH675

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PQQ A 504
ChainResidue
AGLN76
AHIS144
AARG228
AASN229
AGLN231
AGLN246
AGLY247
APRO248
ATYR343
ATRP346
ATHR348
ALEU376
ALYS377
AARG406
AARG408
ACA503
AHDN505
AHOH636

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE HDN A 505
ChainResidue
AHIS144
AARG228
ATYR343
ATRP346
APQQ504
AHOH675
AHOH1008

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 506
ChainResidue
AGLN39
AARG52
ASER59
BGLY58
BHOH3445
BHOH3485

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HDN B 3001
ChainResidue
BHIS144
BGLN168
BARG228
BPQQ3005
BHOH3167
BHOH3290

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 3002
ChainResidue
BGLU253
BTYR263
BHOH3102
BHOH3105
BHOH3124
BHOH3140

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 3003
ChainResidue
BALA269
BTYR271
BASP273
BGLU309
BHOH3101
BHOH3144

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 3004
ChainResidue
BGLY247
BPRO248
BPQQ3005
BHOH3108
BHOH3167

site_idBC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE PQQ B 3005
ChainResidue
BGLN76
BHIS144
BARG228
BASN229
BGLN231
BGLN246
BGLY247
BPRO248
BTYR343
BTRP346
BTHR348
BLEU376
BLYS377
BARG406
BARG408
BHDN3001
BCA3004
BHOH3129
BHOH3412
BHOH3446

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsRegion: {"description":"PQQ"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10508152","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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 2025-12-24

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