Proteins in PDB homologous to 1dliA

19 proteins (109 PDB structures) with E() < 0.001

Homologs in SwissProt

Acc   E.C. E() % id alen 118
1dliAThe First Udp-Glucose Dehydrogenase (Udp1. &T*E&K&N*C*D
1dljAThe First Udp-Glucose Dehydrogenase (Udp1. &T*E&K&N*S*D
3phlA, 3pjgA, 3plnA, 3plrAThe Apo-Form Udp-Glucose 6-Dehydrogenase7.3e-8654.7402 &T*E&K&N*C*D
3pidAThe Apo-Form Udp-Glucose 6-Dehydrogenase7.5e-8654.7402 &T*E&K&N*C*D
2y0eA, 2y0eB, 2y0eC, 2y0eDBcec And The Final Step Of Ugds Reaction1.6e-2727.9387 &T*E&K&N*C*D
2y0cA, 2y0cB, 2y0cC, 2y0cDBcec Mutation Y10s7.3e-2727.6387 &T*E&K&N*C*D
2y0dA, 2y0dB, 2y0dC, 2y0dDBcec Mutation Y10k7.3e-2727.6387 &T*E&K&N*C*D
3gg2A, 3gg2B, 3gg2C, 3gg2DUdp-Glucose 6-Dehydrogenase From Porphyr1.5e-2228.5386 &T*E&K&N*C*D
1mv8A, 1mv8B, 1mv8C, 1mv8D1.55 A A Ternary Complex Of Gdp-Mannose &T*E&K&N*C*D
2o3jA, 2o3jB, 2o3jCCaenorhabditis Elegans Udp-Glucose Dehyd1. &T*E&K&N*C*D
1mfzA, 1mfzB, 1mfzC, 1mfzD, 1muuA, 1muuB, 1muuC, 1muuDPartially Refined 2.8 A Gdp-Mannose Dehy1.1.1.1321.5e-1925.1430 &T*E&K&N*C*D
2q3eA, 2q3eB, 2q3eC, 2q3eD, 2q3eE, 2q3eF, 2q3eG, 2q3eH, 2q3eI, 2q3eJ, 2q3eK, 2q3eL, 2qg4A, 2qg4B, 2qg4C, 2qg4D, 2qg4E, 2qg4F, 2qg4G, 2qg4HHuman Udp-Glucose Dehydrogenase Complexe1. &T*E&K&N*C*D
3tdkA, 3tdkB, 3tdkG, 3tdkH, 3tdkL, 3tdkK, 3tdkF, 3tdkE, 3tdkD, 3tdkC, 3tdkJ, 3tdkIHuman Udp-Glucose Dehydrogenase1. &T*E&K&N*C*D
3prjA, 3prjB, 3prjC, 3prjD, 3prjE, 3prjF, 3ptzA, 3ptzB, 3ptzC, 3ptzD, 3ptzE, 3ptzFRole Of Packing Defects In The Evolution1. &T*E&K&N*C*D
3khuA, 3khuB, 3khuC, 3khuD, 3khuE, 3khuFHuman Udp-Glucose Dehydrogenase Glu161gl1. &T*E&K&N*C*D
3itkA, 3itkB, 3itkC, 3itkD, 3itkE, 3itkFHuman Udp-Glucose Dehydrogenase Thr131al1. &A*E&K&N*C*D
3tf5A, 3tf5B, 3tf5CUdp-Glucose Dehydrogenase V132 Deletion1. &S*E&K&N*C*D
3ojlA, 3ojlB, 3ojoA, 3ojoBNative The Udp-N-Acetyl-Mannosamine Dehy2.6e-1324.6415 &T*P&K&N*C*D
3g79A, 3g79BNdp-N-Acetyl-D-Galactosaminuronic Acid D0.0001423.2383 &T*L&K&N*C*D

Proteins identified as mutant are highlighted in maroon. Conservative changes in active site residues, e.g. &K, are marked in green. Non-conservative changes to active site residues (&A) are highlighted in red. Library sequence residues identical to MACie active site residues are shown in grey.

Likewise, E.C. numbers identical to the MACiE protein are shown in grey; differences in black.

Homologs in PDB for MACiE ID:

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