EC 3.4.23.6 - obsolete, reclassified now as EC 3.4.23.18 - EC 3.4.23.28 and EC 3.4.23.30

3D structures of EC 3.4.23.6 in Protein Data Bank

updated: 6 January 2022, 2:15

1. 6apr: Structures of Complexes of Rhizopuspepsin with Pepstatin and Other Statine-containing Inhibitors
2. 5er2: High-resolution X-ray Diffraction Study of The Complex between Endothiapepsin and an Oligopeptide Inhibitor. The Analysis of The Inhibitor Binding and Description of The Rigid Body Shift in The Enzyme
3. 5er1: A Rational Approach to The Design of Antihypertensives. X- Ray Studies of Complexes between Aspartic Proteinases and Aminoalcohol Renin Inhibitors
4. 5apr: Structures of Complexes of Rhizopuspepsin with Pepstatin and Other Statine-containing Inhibitors
5. 4er4: High-resolution X-ray Analyses of Renin Inhibitor-aspartic Proteinase Complexes
6. 4er2: The Active Site of Aspartic Proteinases
7. 4er1: The Active Site of Aspartic Proteinases
8. 4apr: Structures of Complexes of Rhizopuspepsin with Pepstatin and Other Statine-containing Inhibitors
9. 3er5: The Active Site of Aspartic Proteinases
10. 3er3: The Active Site of Aspartic Proteinases
11. 1uh7: Crystal Structure of Rhizopuspepsin at Ph 4.6
12. 1uh8: Crystal Structure of Rhizopuspepsin at Ph 8.0
13. 1uh9: Crystal Structure of Rhizopuspepsin at Ph 7.0
14. 3apr: Binding of a Reduced Peptide Inhibitor to The Aspartic Proteinase from Rhizopus Chinensis. Implications for a Mechanism of Action
15. 2apr: Structure and Refinement at 1.8 Angstroms Resolution of The Aspartic Proteinase from Rhizopus Chinensis
16. 2er0: X-ray Studies of Aspartic Proteinase-statine Inhibitor Complexes
17. 2er6: The Structure of a Synthetic Pepsin Inhibitor Complexed with Endothiapepsin.
18. 2er7: X-ray Analyses of Aspartic Proteinases.iii. Three- Dimensional Structure of Endothiapepsin Complexed with a Transition-state Isostere Inhibitor of Renin at 1.6 Angstroms Resolution
19. 2er9: X-ray Studies of Aspartic Proteinase-statine Inhibitor Complexes.