 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 5]](hv5263fig5mag.jpg)
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Figure 5
Active site of A. baumannii alanine racemase. (a) 2Fo− Fc electron-density map of the active site contoured at 1.0σ with isomesh map shown (1.6 Å carve). The main-chain and side-chain atoms of the AlrAba active-site residues are depicted as sticks. C atoms are green, O atoms red, N atoms blue, S atoms yellow and phosphates orange. The PLP cofactor is depicted as a ball-and-stick model in which C atoms are coloured black. (b) Superposition of the active-site residues of alanine racemases from A. baumannii (green), B. henselae (blue), P. aeruginosa (red) and E. coli (orange). For A. baumannii, a hybrid view is depicted with residues from monomer B, except for the side chain of His159 which is included from monomer A. The PLP cofactors from each structure are depicted as ball-and-stick models. Primes denote residues contributed by the second monomer. The superposition was performed using the residue ranges stated in Table 2 ![[link]](../../../../../../logos/arrows/f_arr.gif) . This figure was produced in PyMOL (DeLano, 2002). |
![[Figure 5]](hv5263fig5.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
