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Table 2 Local structural alignment of the consensus signature residues for the OMPDCs.

From: Protein function annotation with Structurally Aligned Local Sites of Activity (SALSAs)

Structurally aligned signature active site residues for OMPDC
   β1 β2 β3 β4 β7 β8
  PDB 1 2 3 4 5 6 7 8
  1dbt D11 K33 D60 K62 D65 H88 P182 R215
  1dvj D20 K42 D70 K72 D75 H98 P180 R203
Protein 1dqw D37 K59 D91 K93 D96 H122 P202 R235
  1l2u D22 K44 D71 K73 D76 H99 P189 R222
  2za1 D23 K102 D136 K138 D141 n165 P264 R294
SG 2aqw D23 K105 D139 K141 D144 n168 P267 R297
  1. The first five rows represent previously-characterized OMPDCs. The sixth row is a putative OMPDC from Structural Genomics. The columns represent spatially coincident positions in the structural alignment; these positions are numbered 1-8. Known catalytic residues are shown in boldface. POOL-predicted residues are shown in uppercase; residues not predicted by POOL are shown in lowercase. The beta strand on which each position is located is given at the top of the column, above the position number. The good match between the SG protein and the known OMPDCs suggests common function.