7BR4
Structure of deletion mutant of alpha-glucuronidase (TM0752) from Thermotoga maritima
Summary for 7BR4
Entry DOI | 10.2210/pdb7br4/pdb |
Descriptor | Alpha-glucosidase, putative, MANGANESE (II) ION, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, ... (4 entities in total) |
Functional Keywords | hydrolase-oxidoreductase, alpha-glucuronidase activity, carbohydrate metabolism, nad-binding rossmann-fold, ldh c-terminal domain-like, hydrolase |
Biological source | Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) |
Total number of polymer chains | 1 |
Total formula weight | 57469.06 |
Authors | Manoj, N.,Mohapatra, S.B. (deposition date: 2020-03-26, release date: 2021-03-31, Last modification date: 2023-12-20) |
Primary citation | Mohapatra, S.B.,Manoj, N. A conserved pi-helix plays a key role in thermoadaptation of catalysis in the glycoside hydrolase family 4. Biochim Biophys Acta Proteins Proteom, 1869:140523-140523, 2021 Cited by PubMed: 32853774DOI: 10.1016/j.bbapap.2020.140523 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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