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Figure 1
A comparison of the loop structures of (a) GhTrp (PDB entry 9ect), (b) bovine trypsin (PDB entry 1hj9) and (c) Bacillus intermedius glutamyl-endopeptidase (PDB entry 1p3c). The known specificity loops, loop A (37 loop; dark orange), loop B (60 loop; cyan), loop C (99 loop; yellow), loop D (148 loop; maroon), loop E (75 loop; green), loop 1 (189 loop; magenta), loop 2 (220 loop; light blue) and loop 3 (175 loop; orange), are illustrated in each structure with the remaining protein rendered in grey. In (c), the location of the N-terminus is indicated by the N-terminal leucine residue rendered as a blue stick model. Potential interactions between members of the catalytic triad are rendered as dashed lines and the location of the S1 pocket is annotated. All molecules are presented in an identical orientation.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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