Dynamic, ligand-dependent conformational change triggers reaction of ribose-1,5-bisphosphate isomerase from Thermococcus kodakarensis KOD1.
- Cited forX-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF APOENZYME AND WILD-TYPE IN COMPLEX WITH PRODUCT AND MUTANT SER-133 IN COMPLEX WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT, REACTION MECHANISM, ACTIVE SITES, MUTAGENESIS OF CYS-133; ASP-202 AND ARG-227
- CategoriesFunction, Interaction, Phenotypes & Variants, Structure
- SourceUniProtKB reviewed (Swiss-Prot)