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1JQB

Alcohol Dehydrogenase from Clostridium Beijerinckii: Crystal Structure of Mutant with Enhanced Thermal Stability

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0050009molecular_functionisopropanol dehydrogenase (NADP+) activity
B0008270molecular_functionzinc ion binding
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
B0050009molecular_functionisopropanol dehydrogenase (NADP+) activity
C0008270molecular_functionzinc ion binding
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
C0050009molecular_functionisopropanol dehydrogenase (NADP+) activity
D0008270molecular_functionzinc ion binding
D0016491molecular_functionoxidoreductase activity
D0046872molecular_functionmetal ion binding
D0050009molecular_functionisopropanol dehydrogenase (NADP+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 1353
ChainResidue
ACYS1037
AHIS1059
AASP1150

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 2353
ChainResidue
BCYS2037
BHIS2059
BGLU2060
BASP2150

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN C 3353
ChainResidue
CASP3150
CCYS3037
CHIS3059

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 4353
ChainResidue
DHOH112
DCYS4037
DHIS4059
DASP4150

Functional Information from PROSITE/UniProt
site_idPS00059
Number of Residues15
DetailsADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEaVGEvvevGseV
ChainResidueDetails
AGLY1058-VAL1072

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:12381840, ECO:0000269|PubMed:20102159, ECO:0000269|PubMed:9836873
ChainResidueDetails
ACYS1037
CHIS3059
CGLU3060
CASP3150
DCYS4037
DHIS4059
DGLU4060
DASP4150
AHIS1059
AGLU1060
AASP1150
BCYS2037
BHIS2059
BGLU2060
BASP2150
CCYS3037

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:9836873
ChainResidueDetails
AILE1175
BLYS2340
CILE3175
CGLY3198
CTYR3218
CILE3265
CLYS3340
DILE4175
DGLY4198
DTYR4218
DILE4265
AGLY1198
DLYS4340
ATYR1218
AILE1265
ALYS1340
BILE2175
BGLY2198
BTYR2218
BILE2265

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qlh
ChainResidueDetails
ASER1039
AHIS1042

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qlh
ChainResidueDetails
BHIS2042
BSER2039

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qlh
ChainResidueDetails
CHIS3042
CSER3039

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qlh
ChainResidueDetails
DSER4039
DHIS4042

224572

PDB entries from 2024-09-04

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