 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](aq5005fig1mag.jpg)
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Figure 1
Sequence alignment of P. aeruginosa PA2949 with human ABHD6 and secondary-structure prediction. (a) Sequence alignment. The putative active site comprising the catalytic triad (Ser148, His306 and Asp278 in ABHD6, and Ser137, His286 and Asp258 in PA2949) and the oxyanion-hole residues (Phe80 and Met149 in ABHD6, and Phe71 and Met138 in PA2949) are indicated by red triangles and circles, respectively. Conserved residues (His99 and Asp104 in ABHD6 and His90 and Asp95 in PA2949) of the putative HXXXXD acyltransferase motif are indicated by red squares. The putative transmembrane domains of PA2949 (amino acids 4–24) and ABHD6 (amino acids 9–29) are indicated by red lines above and below the sequences, respectively. Identical and similar residues are shaded in black and yellow, respectively. The pairwise sequence alignment was generated with the EMBOSS Water (Rice et al., 2000  ) local alignment tool from the European Bioinformatics Institute (EMBL–EBI). (b) Secondary structure was predicted with the JPred4 server (Drozdetskiy et al., 2015) using a method based on hidden Markov models. α-Helices are indicated in red and β-sheets in green. |
![[Figure 1]](aq5005fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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