2BZS

Binding of anti-cancer prodrug CB1954 to the activating enzyme NQO2 revealed by the crystal structure of their complex.

Summary for 2BZS

Entry DOI	10.2210/pdb2bzs/pdb
Related	1QR2 1SG0 1ZX1 2QR2
Descriptor	NRH DEHYDROGENASE [QUINONE] 2, ZINC ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
Functional Keywords	oxidoreductase, nqo2, cb1954, fad, flavoprotein, metal-binding, polymorphism, zinc
Biological source	HOMO SAPIENS (HUMAN)
Total number of polymer chains	2
Total formula weight	55126.38
Authors	Abu Khader, M.M.,Heap, J.T.,De Matteis, C.,Kellam, B.,Doughty, S.W.,Minton, N.,Paoli, M. (deposition date: 2005-08-22, release date: 2005-09-23, Last modification date: 2023-12-13)
Primary citation	Abu Khader, M.M.,Heap, J.T.,De Matteis, C.,Kellam, B.,Doughty, S.W.,Minton, N.,Paoli, M. Binding of the Anticancer Prodrug Cb1954 to the Activating Enzyme Nqo2 Revealed by the Crystal Structure of Their Complex. J.Med.Chem., 48:7714-, 2005 Cited by PubMed Abstract: CB1954 is an attractive prodrug for directed-enzyme prodrug therapy (DEPT) and a conventional prodrug against tumors in which the enzyme NQO2 is highly expressed. We have determined the crystal structure of the NQO2-CB1954 complex to 2.0 A resolution. The binding of the prodrug is governed by hydrophobic forces, while two key electrostatic contacts determine the specific orientation of the ligand. The structure also reveals an unfavorable interaction, therefore suggesting possible avenues for DEPT-tailored engineering studies. PubMed: 16302811 DOI: 10.1021/JM050730N PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation