1tmg | pdb_00001tmg

crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 M59F mutant

spinqualitylabelsall models 1tmg, resolution 1.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1tmg is a 2 chain structure with sequence from Bacillus amyloliquefaciens and Hordeum vulgare subsp. vulgare. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.67Å Ligands: 15P, 1PE, CA, CIT, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SUBT_BACAM Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin. 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 A series of mutants of chymotrypsin inhibitor 2 (CI2), at residues that interact with the inhibited enzyme subtilisin BPN', were studied to determine the relative importance of intermolecular contacts on either side of the scissile bond. Mutants were tested for inhibition of subtilisin, rates of hydrolysis by subtilisin, and ability to acylate subtilisin. Additionally, crystal structures of the mutant CI2 complexes with subtilisin were obtained. Ordered water molecules were found to play an important role in inhibitor recognition, and features of the crystal structures, in combination with biochemical data, support a transition-state stabilization role for the P(1) residue in subtilisin catalysis. Consistent with the proposed mechanism of inhibition, in which rapid acylation is followed by religation, leaving-group contacts with the enzyme were found to be more critical determinants of inhibition than acylating-group contacts in the mutants studied here. Binding, proteolytic, and crystallographic analyses of mutations at the protease-inhibitor interface of the subtilisin BPN'/chymotrypsin inhibitor 2 complex.,Radisky ES, Kwan G, Karen Lu CJ, Koshland DE Jr Biochemistry. 2004 Nov 2;43(43):13648-56. PMID:15504027 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chymotrypsin inhibitor 3D structures Subtilisin 3D structures

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