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7UUT

Ternary complex crystal structure of secondary alcohol dehydrogenases from the Thermoanaerobacter ethanolicus mutants C295A and I86A provides better understanding of catalytic mechanism

Replaces:  7JNU
Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0008106molecular_functionalcohol dehydrogenase (NADP+) activity
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0008106molecular_functionalcohol dehydrogenase (NADP+) activity
B0008270molecular_functionzinc ion binding
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0008106molecular_functionalcohol dehydrogenase (NADP+) activity
C0008270molecular_functionzinc ion binding
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0008106molecular_functionalcohol dehydrogenase (NADP+) activity
D0008270molecular_functionzinc ion binding
D0016491molecular_functionoxidoreductase activity
D0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00059
Number of Residues15
DetailsADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEaVGEvvevGseV
ChainResidueDetails
AGLY58-VAL72
BGLY58-VAL72

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:20102159, ECO:0000269|PubMed:9836873
ChainResidueDetails
BCYS37
BHIS59
BASP150
CCYS37
CHIS59
CASP150
DCYS37
DHIS59
DASP150

site_idSWS_FT_FI2
Number of Residues15
DetailsBINDING: BINDING => ECO:0000269|PubMed:9836873
ChainResidueDetails
BILE175
CLYS340
DILE175
DGLY198
DTYR218
DVAL265
DLYS340
BGLY198
BTYR218
BVAL265
BLYS340
CILE175
CGLY198
CTYR218
CVAL265

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PDB entries from 2024-11-06

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