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Proteins in PDB homologous to 1f61A

15 proteins (106 PDB structures) with E() < 0.001

Homologs in SwissProt


Acc   E.C. E() % id alen 180
&H
191
*C
193
*H
228
&R
315
&S
317
&S
1f61A, 1f61B, 1f8mA, 1f8mB, 1f8mC, 1f8mDIsocitrate Lyase From Mycobacterium Tube4.1.3.17.3e-185100.0418 &H*C*H&R&S&S
1f8iA, 1f8iB, 1f8iC, 1f8iDIsocitrate Lyase:nitropropionate:glyoxyl4.1.3.16.9e-18499.8418 &H*S*H&R&S&S
3i4eA, 3i4eB, 3i4eC, 3i4eDIsocitrate Lyase From Burkholderia Pseud1.6e-12667.0415 &H*C*H&R&S&S
3e5bA, 3e5bB, 3e5bC, 3e5bD, 3oq8A, 3oq8B, 3oq8C, 3oq8D, 3p0xA, 3p0xB, 3p0xC, 3p0xD2.4 A Isocitrate Lyase From Brucella Mel5.9e-11766.8401 &H*C*H&R&S&S
3eolA, 3eolB2.0a Isocitrate Lyase From Brucella Meli2.5e-11666.6401 &H*C*H&R&S&S
1igwA, 1igwB, 1igwC, 1igwDThe Isocitrate Lyase From The A219c Muta4.1.3.11.8e-10961.0421 &H*C*H&R&S&S
3lg3A, 3lg3B1.4a Isocitrate Lyase From Yersinia Pest2.4e-10558.1425 &H*C*H&R&S&S
1dquAThe Isocitrate Lyase From Aspergillus Ni4.1.3.13.1e-4732.7511 &H*C*H&R&S&S
3eooA, 3eooB, 3eooC, 3eooD, 3eooE, 3eooF, 3eooG, 3eooH, 3eooI, 3eooJ, 3eooK, 3eooL, 3eooM, 3eooN, 3eooO, 3eooP2.9a Methyl-Isocitrate Lyase From Burkho7e-1127.1332 &H*C*H&R&T&L
1zlpA, 1zlpBPetal Death Protein Psr132 With Cysteine3.7.1.1, 4.1.3.221.1e-1032.2205 &F*C*H&R----
1mumA, 1mumB, 1oqfA, 1oqfBThe 2-Methylisocitrate Lyase (Prpb) From4.1.3.301.6e-1028.2291 &H*C*H&R&T&L
1xg3A, 1xg3B, 1xg3C, 1xg3D, 1xg4A, 1xg4B, 1xg4C, 1xg4DThe C123s 2-Methylisocitrate Lyase Mutan4.1.3.301.5e-0927.8291 &H*S*H&R&T&L
1ujqA, 1ujqB, 1ujqC, 1ujqD, 1o5qA, 1o5qB, 1o5qC, 1o5qD2-Methylisocitrate Lyase (Prpb) From Sal4.1.3.306.6e-0931.5184 &H*C*H&R----
3fa3A, 3fa3B, 3fa3C, 3fa3D, 3fa3E, 3fa3F, 3fa3G, 3fa3H, 3fa3I, 3fa3J, 3fa3K, 3fa3L, 3fa3M, 3fa3N, 3fa3O, 3fa3P, 3fa4A, 3fa4B, 3fa4C, 3fa4D, 3fa4E, 3fa4F, 3fa4G, 3fa4H, 3fa4I, 3fa4J, 3fa4K, 3fa4L2,3-Dimethylmalate Lyase, A Pep MutaseIS1.1e-0832.3167 &H*C*H&R----
3lyeA, 3m0jA, 3m0kAOxaloacetate Acetylhydrolase7.5e-0828.0236 &H*C*H&R----

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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