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Proteins in PDB homologous to 1g8kA

Additional 1g8k chains
1g8kB

19 proteins (58 PDB structures) with E() < 0.001

Homologs in SwissProt


Acc   E.C. E() % id alen 24
*C
98
%S
99
%S
238
%S
1g8kA, 1g8kC, 1g8kE, 1g8kGCrystal Structure Analysis Of Arsenite O1.20.98.10100.0822 *C%S%S%S
1g8jA, 1g8jCCrystal Structure Analysis Of Arsenite O1.20.98.1099.8822 *C%S%S%S
2napA, 2jimA, 2jipA, 2jirA, 2v45ADissimilatory Nitrate Reductase (Nap) Fr1.7.99.41.4e-1923.8778 --%L%C%A
2jioA, 2jiqA, 2v3vAA New Catalytic Mechanism Of Periplasmic1.7.99.41.6e-1923.8778 --%L%C%A
2nyaA, 2nyaFThe Periplasmic Nitrate Reductase (Nap) 1.7.99.42.5e-1823.9771 --%N%C%M
2iv2X, 1aa6A, 1fdiA, 1fdoAReinterpretation Of Reduced Form Of Form1.2.1.24.4e-1521.9702 ------%S
3ml1AThe Periplasmic Nitrate Reductase From C1.7.99.45.3e-1522.8799 --%N%C%M
3o5aAPartially Reduced Periplasmic Nitrate Re1.7.99.45.3e-1522.8799 --%N%C%M
1ogyA, 1ogyC, 1ogyE, 1ogyG, 1ogyI, 1ogyK, 1ogyM, 1ogyOThe Heterodimeric Nitrate Reductase From1.7.99.41.3e-1222.3782 --%N%C%M
1dmsADmso Reductase1.7.2.38.4e-1022.7743 ------%S
2vpwA, 2vpwE, 2vpxA, 2vpxE, 2vpyA, 2vpyE, 2vpzA, 2vpzEPolysulfide Reductase With Bound Menaqui3e-0922.6674 ------%D
1e18ATungsten-Susbstituted Dmso Reductase Fro1.7.2.32.4e-0822.4786 --%S%P%S
1e5vA, 1e5vC, 1h5nA, 1h5nC, 1dmrA, 2dmrA, 3dmrAOxidized Dmso Reductase Exposed To Hepes1.7.2.33.8e-0822.3786 --%S%P%S
1e60A, 1e60C, 1e61A, 1e61COxidized Dmso Reductase Exposed To Hepes1.7.2.34.5e-0822.3786 --%S%P%S
4dmrAReduced Dmso Reductase From Rhodobacter 1.7.2.35.3e-0822.3786 --%S%P%S
1kqfA, 1kqgAFormate Dehydrogenase N From E. Coli1.2.1.20.0001123.5336 --%L%C%A
2e7zAAcetylene Hydratase From Pelobacter Acet0.0001820.9705 --%D%T--
1tmoATrimethylamine N-Oxide Reductase From Sh1.7.2.30.000321.1757 ------%Q
1eu1AThe Rhodobacter Sphaeroides Dimethylsulf0.0008422.4673 --------

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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