2EA3
Crystal Structure Of Cellulomonas Bogoriensis Chymotrypsin
Summary for 2EA3
Entry DOI | 10.2210/pdb2ea3/pdb |
Descriptor | Chymotrypsin, SULFATE ION (3 entities in total) |
Functional Keywords | celloulomonas, chymotrypsin, protease, hydrolase |
Biological source | Cellulomonas bogoriensis |
Total number of polymer chains | 1 |
Total formula weight | 19078.85 |
Authors | |
Primary citation | Shaw, A.,Saldajeno, M.L.,Kolkman, M.A.,Jones, B.E.,Bott, R. Structure determination and analysis of a bacterial chymotrypsin from Cellulomonas bogoriensis Acta Crystallogr.,Sect.F, 63:266-269, 2007 Cited by PubMed Abstract: The crystal structure of a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis has been determined using data to 1.78 A resolution and refined to a crystallographic R factor of 0.167. The crystal structure reveals a large P1 substrate-specificity pocket, as expected for chymotrypsins. The structure is compared with close structural homologues. This comparison does not reveal clear reasons for the alkali tolerance of the enzyme, but the greater compactness of the structure and lowered hydrogen bonding may play a role. PubMed: 17401191DOI: 10.1107/S1744309107008937 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.78 Å) |
Structure validation
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