2er6 | pdb_00002er6
THE STRUCTURE OF A SYNTHETIC PEPSIN INHIBITOR COMPLEXED WITH ENDOTHIAPEPSIN.
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Overview
The conformation of a synthetic polypeptide inhibitor, bound to the active, site of the fungal aspartic proteinase endothiapepsin (EC 3.4.23.6), has, been determined by X-ray diffraction at 0.20-nm resolution and refined to, an agreement factor of 0.20. The inhibitor: Pro Thr Glu Phe-R-Phe Arg Glu, (R = -CH2NH-) is based on a chromogenic substrate of pepsin (EC 3.4.23.1)., It has, in place of the scissile bond, a reduced peptide group which is, resistant to hydrolysis and mimics the tetrahedral transition state. The, inhibitor binds in an extended conformation with the reduced bond close to, the essential aspartate side-chains of the enzyme. The hydrogen bonds and, hydrophobic interactions between the enzyme and the inhibitor do not, induce large conformational changes.
About this Structure
2ER6 is a Single protein structure of sequence from Cryphonectria parasitica. Active as Hydrolase, with EC number 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 Full crystallographic information is available from OCA.
Reference
The structure of a synthetic pepsin inhibitor complexed with endothiapepsin., Cooper J, Foundling S, Hemmings A, Blundell T, Jones DM, Hallett A, Szelke M, Eur J Biochem. 1987 Nov 16;169(1):215-21. PMID:3119339
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