4LP9
Endothiapepsin complexed with Phe-reduced-Tyr peptide.
Summary for 4LP9
| Entry DOI | 10.2210/pdb4lp9/pdb |
| Related | 1GVT 1GVU 1GVV 1GVW 1GVX |
| Related PRD ID | PRD_001157 |
| Descriptor | Endothiapepsin, Ser-Leu-Phe-His-Phenylalanyl-reduced-peptide-bond-Tyrosyl-Thr-Pro, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | aspartic proteinase fold, proteolysis, hydrolase (acid proteinase), hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Cryphonectria parasitica (Chesnut blight fungus) |
| Total number of polymer chains | 2 |
| Total formula weight | 35652.76 |
| Authors | Guo, J.,Cooper, J.B.,Wood, S.P. (deposition date: 2013-07-15, release date: 2014-01-15, Last modification date: 2024-11-20) |
| Primary citation | Guo, J.,Cooper, J.B.,Wood, S.P. The structure of endothiapepsin complexed with a Phe-Tyr reduced-bond inhibitor at 1.35 angstrom resolution. Acta Crystallogr F Struct Biol Commun, 70:30-33, 2014 Cited by PubMed Abstract: Endothiapepsin is a typical member of the aspartic proteinase family. The catalytic mechanism of this family is attributed to two conserved catalytic aspartate residues, which coordinate the hydrolysis of a peptide bond. An oligopeptide inhibitor (IC50 = 0.62 µM) based on a reduced-bond transition-state inhibitor of mucorpepsin was co-crystallized with endothiapepsin and the crystal structure of the enzyme-inhibitor complex was determined at 1.35 Å resolution. A total of 12 hydrogen bonds between the inhibitor and the active-site residues were identified. The resulting structure demonstrates a number of novel subsite interactions in the active-site cleft. PubMed: 24419612DOI: 10.1107/S2053230X13032974 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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