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Figure 2
X-ray crystallographic structure determination of inhibitors EA3-3 and EA5-3 binding to CA II and chimeric CA IX (a multiple amino acid mutant of CA II mimicking amino acids of the CA IX active site). The electron density of the inhibitors is shown in green. Amino acids that were mutated in CA II to reproduce the CA IX active site are also shown, as well as histidine residues coordinating the Zn2+ ion. Electron-density maps were calculated in the absence of inhibitors. The 2Fo − Fc map contoured at 1σ is gray, while the difference map Fo − Fc contoured at 3σ is green. Residues of chCA IX are colored green and CA II is yellow. The inhibitors are light gray. The Zn2+ ion is shown as a gray sphere and water molecules are shown as red spheres.

IUCrJ
Volume 11| Part 4| July 2024| Pages 556-569
ISSN: 2052-2525
https://doi.org/10.1107/S2052252524004627