PDBsum entry 2eu2

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Lyase PDB id
Protein chain
257 a.a.
Waters ×310

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Title X-Ray crystallographic studies reveal that the incorporation of spacer groups in carbonic anhydrase inhibitors causes alternate binding modes.
Authors S.Z.Fisher, L.Govindasamy, N.Boyle, M.Agbandje-Mckenna, D.N.Silverman, G.M.Blackburn, R.Mckenna.
Ref. Acta Crystallogr.,Sect.F, 2006, 62, 618-622. [DOI no: 10.1107/S1744309106020446]
PubMed id 16820676
Human carbonic anhydrases (CAs) are well studied targets for the development of inhibitors for pharmaceutical applications. The crystal structure of human CA II has been determined in complex with two CA inhibitors (CAIs) containing conventional sulfonamide and thiadiazole moieties separated by a -CF2- or -CHNH2- spacer group. The structures presented here reveal that these spacer groups allow novel binding modes for the thiadiazole moiety compared with conventional CAIs.
Figure 2.
Figure 2 Interactions between HCA II and inhibitors. (a) BB3, (b) TDM. Hydrogen bonds are indicated by dashed red lines (distances given in Å), side chains are as labeled and the Zn atom is shown as a black sphere. Figures were generated and rendered with BobScript and Raster3D, respectively (Esnouf, 1999[Esnouf, R. M. (1999). Acta Cryst. D55, 938-940.]; Merritt & Bacon, 1997[Merritt, E. A. & Bacon, D. J. (1997). Methods Enzymol. 277, 505-524.]).
The above figure is reprinted from an Open Access publication published by the IUCr: Acta Crystallograph Sect F Struct Biol Cryst Commun (2006, 62, 618-622) copyright 2006.
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