 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](rl5206fig2mag.jpg)
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Figure 2
Interactions of CA in the active site. The Cα atoms of CA are in lime green and those of the protein are in tan. The two zinc ions are in gray. (b) The electron density around CA and the two zinc ions in gray corresponds to the 2mFo − DFc map, and the contour level is 0.9σ. The electron density confirms that the ligand is CA. (c) Interactions of Ser143 and Val144 with the protein in both loop-in and loop-out conformations. The two conformations of the flexible loop are shown in tan for the loop-in conformation and in dark cyan for the loop-out conformation. The loops are exhibited as polyalanine chains, except for Ser143 and Val144 for the loop-in conformation and Ser143, Val144 and Leu147 for the loop-out conformation. The protein residues that interact with the loop atoms are shown in hot pink unless they are also part of the loop. The substrate CA is shown in lime green. Hydrogen bonds are shown by dashed lines. Two hydrogen bonds to the protein (Asn89 ND2⋯Val144 O and Asn275 ND2⋯Ser143 OG) and one to CA (Ser143 OG⋯CA424 O5) are made for the loop-in conformation and contacts with His168, His306 and the α-carboxylate of CA (see Supplementary Tables S2 and S3). Three intraloop hydrogen bonds are made in the loop-out conformation (Ser143 OG⋯Leu147 O, Ser143 N⋯Leu147 O and Leu147 N⋯Val144 O) and contacts with Phe139 and Leu147, and with Asn89, Lys91 and Pro93 of loop 2 (see Supplementary Table S3). |
![[Figure 2]](rl5206fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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