Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7XY9

Cryo-EM structure of secondary alcohol dehydrogenases TbSADH after carrier-free immobilization based on weak intermolecular interactions

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 PROSITE/UniProt
site_idPS00059
Number of Residues15
DetailsADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEaVGEvvevGseV
ChainResidueDetails
AGLY58-VAL72

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:20102159, ECO:0000269|PubMed:9836873
ChainResidueDetails
ACYS37
DCYS37
DHIS59
DASP150
AHIS59
AASP150
BCYS37
BHIS59
BASP150
CCYS37
CHIS59
CASP150

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:9836873
ChainResidueDetails
AILE175
BLYS340
CILE175
CGLY198
CTYR218
CVAL265
CLYS340
DILE175
DGLY198
DTYR218
DVAL265
AGLY198
DLYS340
ATYR218
AVAL265
ALYS340
BILE175
BGLY198
BTYR218
BVAL265

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon