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Proteins in PDB homologous to 1n62B

25 proteins (126 PDB structures) with E() < 0.001

Homologs in SwissProt


Acc   E.C. E() % id alen 388
&C
763
*E
1n5wB, 1n5wE, 1n60B, 1n60E, 1n61B, 1n61E, 1n62B, 1n62E, 1n63B, 1n63EThe Cu,Mo-Co Dehydrogenase (Codh); Oxidi1.2.99.20100.0804 &C*E
1zxiB, 1zxiEReconstituted Co Dehydrogenase From Olig1.2.99.2099.9804 &C*E
1ffuB, 1ffuE, 1ffvB, 1ffvECarbon Monoxide Dehydrogenase From Hydro1.2.99.2068.7788 &X*E
1t3qB, 1t3qEQuinoline 2-Oxidoreductase From Pseudomo3.1e-9033.8797 --*E
1rm6A, 1rm6D, 1sb3A, 1sb3D4-Hydroxybenzoyl-Coa Reductase From Thau1.3.7.95.9e-4927.7773 --*E
1sijA, 1vlbA, 3fahA, 3fc4A, 3l4pAThe Aldehyde Dehydrogenase (A.K.A. Aor O1.2.99.71.3e-3626.7776 --*E
3hrdA, 3hrdENicotinate Dehydrogenase1.17.1.55.2e-3029.5447 ----
1jroB, 1jroD, 1jroF, 1jroH, 1jrpB, 1jrpD, 1jrpF, 1jrpH, 2w3rB, 2w3rD, 2w3rF, 2w3rH, 2w3sB, 2w3sD, 2w3sF, 2w3sH, 2w54B, 2w54D, 2w54F, 2w54HXanthine Dehydrogenase From Rhodobacter 6.6e-3025.3786 --*E
2w55B, 2w55D, 2w55F, 2w55HXanthine Dehydrogenase (E232q Variant) F6.6e-3025.3786 --*E
3sr6C, 3sr6LReduced Bovine Xanthine Oxidase In Compl1.17.1.4, 1.17.3.22e-2726.1771 --*E
3etrC, 3etrN, 3ns1C, 3ns1L, 3nvvC, 3nvvL, 3nvzC, 3nvzLXanthine Oxidase In Complex With Lumazin1.17.1.4, 1.17.3.22e-2726.1771 --*E
3nrzC, 3nrzL, 3nvwC, 3nvwL, 3nvyC, 3nvyLBovine Xanthine Oxidase In Complex With 1.17.1.4, 1.17.3.22e-2726.1771 --*E
3eubC, 3eubL, 3eubU, 3eub4Desulfo-Xanthine Oxidase With Xanthine1.17.1.4, 1.17.3.22.1e-2726.1771 --*E
1fiqC, 3b9jC, 3b9jKXanthine Oxidase From Bovine Milk1.17.1.4, 1.17.3.22.1e-2726.1771 --*E
1n5xA, 1n5xBXanthine Dehydrogenase From Bovine Milk 1.17.1.4, 1.17.3.24.7e-2726.1771 --*E
1fo4A, 1fo4B, 1v97A, 1v97B, 1vdvA, 1vdvB, 3bdjA, 3bdjB, 3am9A, 3am9B, 3amzA, 3amzB, 3ax7A, 3ax7B, 3ax9A, 3ax9BXanthine Dehydrogenase Isolated From Bov1.17.1.4, 1.17.3.24.7e-2726.1771 --*E
3unaA, 3unaB, 3uncA, 3uncB, 3uniA, 3uniBBovine Milk Xanthine Dehydrogenase With 1.17.1.4, 1.17.3.24.7e-2726.1771 --*E
1dgjAThe Aldehyde Oxidoreductase From Desulfo6.9e-2724.1796 --*E
2e1qA, 2e1qB, 2e1qC, 2e1qDHuman Xanthine Oxidoreductase Mutant, Gl1.17.1.4, 1.17.3.22.7e-2625.4769 --*E
2ckjA, 2ckjB, 2ckjC, 2ckjDHuman Milk Xanthine Oxidoreductase1.17.1.4, 1.17.3.29.8e-2625.2769 --*E
3an1A, 3an1BRat D428a Mutant, Urate Bound Form1.17.1.4, 1.17.3.28.6e-2423.9785 --*E
2e3tA, 2e3tBRat Xanthine Oxidoreductase Mutant (W3351.17.1.4, 1.17.3.28.6e-2423.9785 --*E
1wygAA Rat Xanthine Dehydrogenase Triple Muta1.17.1.4, 1.17.3.21e-2323.9785 --*E
3zyvA, 3zyvB, 3zyvC, 3zyvDThe Mouse Liver Aldehyde Oxidase 3 (maox1.6e-2022.7763 --*E
3hrdB, 3hrdFNicotinate Dehydrogenase1.17.1.54e-1928.0307 --*E

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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