 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 3]](wd5199fig3mag.jpg)
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Figure 3
Illustration of the differences in the conformation of the N-terminus of bovine chymosin (a) and camel chymosin (b) in relation to the central β-sheet. The view is from the N-terminal domain towards the C-terminal domain. The active-site residues and the activated water molecule are shown in red and the N-terminal residues up to and including Tyr16 are shown in magenta. The side chain of Ser94 is shown in red/blue and the hydrogen bond formed to the β-sheet in camel chymosin is marked in yellow. The chloride ion in bovine chymosin is illustrated as a green sphere and the glycerol (Gol1334) in camel chymosin is shown in stick representation. (c) Enlargement of the environment of Val6 (within 5 Å) in bovine chymosin, where Phe33, Val93, Leu166, Leu168 and solvent interact with the side chain. The sequence and charge of residues 1–16 in camel and bovine chymosin at pH 6.65 are shown in the box, noting that camel chymosin lacks residues 1–3. (d) The electron density in the active site of camel chymosin corresponding to the two active-site Asp residues, the activated water molecule, Tyr11 and glycerol (Gol1334). The electron density is traced at the 1.0σ level. |
![[Figure 3]](wd5199fig3.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
