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. 2011 Jun 24;6(6):e21532. doi: 10.1371/journal.pone.0021532

Figure 3. Amino acid sequence alignment of rhinocerases with other viper venom serine protease homologues.

Figure 3

The alignment was created using ClustalW [12] and the figure was generated using GeneDoc [14]. The sequence of bovine α-chymotrypsinogen (NCBI accession number: P00766) (BT-CHY) was included to allow conventional serine protease residue numbering to be assigned. The catalytic triad residues are coloured red, the primary specificity pocket residues are coloured blue and residue 193, involved in the oxyanion hole is coloured green. BG-SP1: AAR24534; BG-RHIN2: CBM40645; BG-RHIN3: CBM40646; EO-SP: ADE45141; ML-P2: Q9PT40; TF-SP2: O13057; TJ-SPH: B0ZT25; TG-SP2A: O13060; VS-KNH7: Q71Q10; VS-SPH1: QAY82; TJ-SP1: Q9DF68; VS-KNH4: Q71QJ4; BJu-SPH: Q7T229; BJa-HP3: Q5W958; ML-P3 and ML-P4 from [5]; Bas-SPL: Q072L6; BG-RHIN4: CBM40647; BG-RHIN5: CBM40648.