1j71

Structure of the extracellular aspartic proteinase from Candida tropicalis yeast.Structure of the extracellular aspartic proteinase from Candida tropicalis yeast.

Structural highlights 1j71 is a 2 chain structure with sequence from Candida tropicalis and Unidentified. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CARP_CANTR Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The crystal structure of the secreted aspartic proteinase from Candida tropicalis yeast (SAPT) has been determined to 1.8 A resolution. The classic aspartic proteinase bilobal structure and domain topology is conserved in SAPT, with the substrate binding cleft situated between the two domains. Structural comparisons made with pepsin indicate that insertions and deletions in the primary sequence modify the SAPT structure to create a more spacious substrate binding cleft with altered specificity. An unexpected tetrapeptide has been found to occupy binding sites S1'-S3', and this suggests the order of release of peptide products in the catalytic mechanism of these enzymes. Structural features are considered with regard to previous substrate specificity data. High-resolution structure of the extracellular aspartic proteinase from Candida tropicalis yeast.,Symersky J, Monod M, Foundling SI Biochemistry. 1997 Oct 21;36(42):12700-10. PMID:9335526 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pepsin Proteinase 3D structures

spinqualitylabelsall models 1j71, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image