1BIL
CRYSTALLOGRAPHIC STUDIES ON THE BINDING MODES OF P2-P3 BUTANEDIAMIDE RENIN INHIBITORS
Summary for 1BIL
| Entry DOI | 10.2210/pdb1bil/pdb |
| Descriptor | Renin, (2S)-2-[(2-amino-1,3-thiazol-4-yl)methyl]-N~1~-[(1S,2R,3R)-1-(cyclohexylmethyl)-2,3-dihydroxy-5-methylhexyl]-N~4~-[2-(d imethylamino)-2-oxoethyl]-N~4~-[(1S)-1-phenylethyl]butanediamide (3 entities in total) |
| Functional Keywords | aspartic proteinase, aspartyl protease, cleavage on pair of basic residues, disease mutation, disulfide bond, glycoprotein, hydrolase, membrane, protease, secreted, zymogen, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 75166.95 |
| Authors | Tong, L. (deposition date: 1995-09-27, release date: 1996-01-29, Last modification date: 2024-10-16) |
| Primary citation | Tong, L.,Pav, S.,Lamarre, D.,Simoneau, B.,Lavallee, P.,Jung, G. Crystallographic studies on the binding modes of P2-P3 butanediamide renin inhibitors. J.Biol.Chem., 270:29520-29524, 1995 Cited by PubMed Abstract: The binding modes of three peptidomimetic P2-P3 butanediamide renin inhibitors have been determined by x-ray crystallography. The inhibitors are bound with their backbones in an extended conformation, and their side chains occupying the S5 to S1' pockets. A (2-amino-4-thiazolyl)methyl side chain at the P2 position shows stronger hydrogen-bonding and van der Waals interactions with renin than the His side chain, which is present in the natural substrate. The ACHPA-gamma-lactam transition state analog has similar interactions with renin as the dihydroxyethylene transition state analog. PubMed: 7493993DOI: 10.1074/jbc.270.49.29520 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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