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Proteins in PDB homologous to 1onwA

11 proteins (64 PDB structures) with E() < 0.001

Homologs in SwissProt


Acc   E.C. E() % id alen 285
*D
1onwA, 1onwB, 1onxA, 1onxB, 1po9A, 1po9B, 1pojA, 1pojB, 1pokB, 1pokAIsoaspartyl Dipeptidase From E. Coli1.2e-16396.7389 *D
2aqoA, 2aqoBE. Coli Isoaspartyl Dipeptidase Mutant E2.2e-16396.4389 *D
2aqvA, 2aqvBE. Coli Isoaspartyl Dipeptidase Mutant Y2.2e-16396.4389 *D
1ybqBEscherichia Coli Isoaspartyl Dipeptidase3.1e-16396.4389 *N
1ybqAEscherichia Coli Isoaspartyl Dipeptidase3.1e-16396.1389 *N
3mpgA, 3mpgBDihydroorotase From Bacillus Anthracis3.5.2.35.1e-0534.798 --
3d6nAAquifex Dihydroorotase Activated By Aspa3.5.2.30.0001340.085 --
1xrfA, 1xrtA, 1xrtBThe A Novel, Latent Dihydroorotase From 3.5.2.30.0001540.085 --
3n2cA, 3n2cB, 3n2cC, 3n2cD, 3n2cE, 3n2cF, 3n2cG, 3n2cH, 3n2cI, 3n2cJ, 3n2cK, 3n2cL, 3n2cM, 3n2cN, 3n2cO, 3n2cPProlidase Eah89906 Complexed With N- Met0.000322.1429 *K
3feqA, 3feqB, 3feqC, 3feqD, 3feqE, 3feqF, 3feqG, 3feqH, 3feqI, 3feqJ, 3feqK, 3feqL, 3feqM, 3feqN, 3feqO, 3feqPUncharacterized Protein Eah899060.0003622.1429 *K
2vunA, 2vunB, 2vunC, 2vunDThe Enamidase At 1.9 A Resolution - A Ne3.5.2.180.0005223.2349 *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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