4YDF

Crystal structure of compound 9 in complex with HTLV-1 Protease

Summary for 4YDF

Entry DOI	10.2210/pdb4ydf/pdb
Related	3LIX 3WSJ
Descriptor	HTLV-1 Protease, N-benzyl-N-[(3S,4S)-4-{benzyl[(4-nitrophenyl)sulfonyl]amino}pyrrolidin-3-yl]-3-nitrobenzenesulfonamide, SULFATE ION, ... (4 entities in total)
Functional Keywords	htlv-1 protease, hydrolase
Biological source	Human T-lymphotropic virus 1
Total number of polymer chains	2
Total formula weight	25880.93
Authors	Kuhnert, M.,Blum, A.,Steuber, H.,Diederich, W.E. (deposition date: 2015-02-22, release date: 2016-02-03, Last modification date: 2024-01-10)
Primary citation	Kuhnert, M.,Blum, A.,Steuber, H.,Diederich, W.E. Privileged Structures Meet Human T-Cell Leukemia Virus-1 (HTLV-1): C2-Symmetric 3,4-Disubstituted Pyrrolidines as Nonpeptidic HTLV-1 Protease Inhibitors. J.Med.Chem., 58:4845-4850, 2015 Cited by PubMed Abstract: 3,4-disubstituted pyrrolidines originally designed to inhibit the closely related HIV-1 protease were evaluated as privileged structures against HTLV-1 protease (HTLV-1 PR). The most potent inhibitor of this series exhibits two-digit nanomolar affinity and represents, to the best of our knowledge, the most potent nonpeptidic inhibitor of HTLV-1 PR described so far. The X-ray structures of two representatives bound to HTLV-1 PR were determined, and the structural basis of their affinity is discussed. PubMed: 26000468 DOI: 10.1021/acs.jmedchem.5b00346 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.804 Å)

Structure validation