Summary for 4L9A
| Entry DOI | 10.2210/pdb4l9a/pdb |
| Descriptor | Putative uncharacterized protein Smu.1393c, GLYCEROL (3 entities in total) |
| Functional Keywords | alpha/beta hydrolase, carboxylesterase, hydrolase |
| Biological source | Streptococcus mutans |
| Total number of polymer chains | 2 |
| Total formula weight | 66975.73 |
| Authors | |
| Primary citation | Wang, Z.,Li, L.,Su, X.D. Structural and functional characterization of a novel alpha / beta hydrolase from cariogenic pathogen Streptococcus mutans. Proteins, 82:695-700, 2014 Cited by PubMed Abstract: The protein Smu.1393c from Streptococcus mutans is annotated as a putative α/β hydrolase, but it has low sequence identity to the structure-known α/β hydrolases. Here we present the crystal structure of Smu.1393c at 2.0 Å resolution. Smu.1393c has a fully open alkaline substrate pocket, whose conformation is unique among other similar hydrolase structures. Three residues, Ser101, His251, and Glu125, were identified as the active center of Smu.1393c. By screening a series of artificial hydrolase substrates, we demonstrated Smu.1393c had low carboxylesterase activity towards short-chain carboxyl esters, which provided a clue for exploring the in vivo function of Smu.1393c. PubMed: 24115105DOI: 10.1002/prot.24418 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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