4Q2K
Bovine alpha chymotrypsin bound to a cyclic peptide inhibitor, 5b
Summary for 4Q2K
| Entry DOI | 10.2210/pdb4q2k/pdb |
| Descriptor | Chymotrypsinogen A, (11S)-4,9-dioxo-N-[(2S)-1-oxo-3-phenylpropan-2-yl]-17,22-dioxa-10,30-diazatetracyclo[21.2.2.2~13,16~.1~5,8~]triaconta-1(25),5,7,13,15,23,26,28-octaene-11-carboxamide (3 entities in total) |
| Functional Keywords | chymotrypsin, protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Bos taurus (bovine) |
| Cellular location | Secreted, extracellular space: P00766 |
| Total number of polymer chains | 4 |
| Total formula weight | 105174.93 |
| Authors | Chan, H.Y.,Bruning, J.B.,Abell, A.D. (deposition date: 2014-04-09, release date: 2014-07-23, Last modification date: 2023-11-08) |
| Primary citation | Chua, K.C.,Pietsch, M.,Zhang, X.,Hautmann, S.,Chan, H.Y.,Bruning, J.B.,Gutschow, M.,Abell, A.D. Macrocyclic protease inhibitors with reduced peptide character. Angew.Chem.Int.Ed.Engl., 53:7828-7831, 2014 Cited by PubMed Abstract: There is a real need for simple structures that define a β-strand conformation, a secondary structure that is central to peptide-protein interactions. For example, protease substrates and inhibitors almost universally adopt this geometry on active site binding. A planar pyrrole is used to replace two amino acids of a peptide backbone to generate a simple macrocycle that retains the required geometry for active site binding. The resulting β-strand templates have reduced peptide character and provide potent protease inhibitors with the attachment of an appropriate amino aldehyde to the C-terminus. Picomolar inhibitors of cathepsin L and S are reported and the mode of binding of one example to the model protease chymotrypsin is defined by X-ray crystallography. PubMed: 24903745DOI: 10.1002/anie.201404301 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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