Table 2

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

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


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.

Wang et al. BMC Bioinformatics 2013 14(Suppl 3):S13   doi:10.1186/1471-2105-14-S3-S13

Open Data