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: 32853774 DOI: 10.1016/j.bbapap.2020.140523 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.95 Å)

Structure validation