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Proteins in PDB homologous to 1ndoA

Additional 1ndo chains
1ndoE

17 proteins (141 PDB structures) with E() < 0.001

Homologs in SwissProt


Acc   E.C. E() % id alen 104
*H
1ndoA, 1ndoC, 1ndoE, 1eg9A, 1o7mA, 1o7nA, 1o7pA, 1o7wA, 1o7gA, 1o7hA, 1uuvA, 1uuwA, 2hmkA, 2hmmA, 2hmoANapthalene 1,2-Dioxygenase1.14.12.122.6e-207100.0447 *H
2hmjA, 2hmlA, 2hmnAThe Naphthalene 1,2-Dioxygenase Phe-352-1.14.12.121.1e-20699.8447 *H
2bmoA, 2bmqA, 2bmrAThe Nitrobenzene Dioxygenase1.1e-17381.9447 *H
2gbwA, 2gbwC, 2gbwE, 2gbxA, 2gbxC, 2gbxEBiphenyl 2,3-Dioxygenase From Sphingomon1.5e-8243.0440 *H
2ckfA, 2ckfC, 2ckfEThe Terminal Component Of The Pah- Hydro9.2e-7942.0440 *H
3en1A, 3eqqAToluene 2,3-Dioxygenase1.14.12.11, 1.14.12.32.3e-5435.5417 *H
1uliA, 1uliC, 1uliE, 1uljA, 1uljC, 1uljEBiphenyl Dioxygenase (bpha1a2) Derived F3.1e-5333.5433 *H
1wqlACumene Dioxygenase (Cuma1a2) From Pseudo3.4e-5134.4439 *H
2xshA, 2xshC, 2xshE, 2xshG, 2xshI, 2xshK, 2xsoA, 2xsoC, 2xsoE, 2xsoG, 2xsoI, 2xsoK, 2xsoM, 2xsoO, 2xsoQ, 2xsoS, 2xsoU, 2xsoWP4 Variant Of Biphenyl Dioxygenase From 1.14.12.185.6e-5133.8438 *H
2xr8A, 2xr8C, 2xr8E, 2xr8G, 2xr8I, 2xr8K, 2xr8M, 2xr8O, 2xr8Q, 2xr8S, 2xr8U, 2xr8W, 2xrxA, 2xrxC, 2xrxE, 2xrxG, 2xrxI, 2xrxK, 2xrxM, 2xrxO, 2xrxQ, 2xrxS, 2xrxU, 2xrxWBiphenyl Dioxygenase From Burkholderia X1.14.12.186.6e-5133.8438 *H
2yfiA, 2yfiC, 2yfiE, 2yfiG, 2yfiI, 2yfiK, 2yfjA, 2yfjC, 2yfjE, 2yfjG, 2yfjI, 2yfjK, 2yflA, 2yflC, 2yflE, 2yflG, 2yflI, 2yflKBiphenyl Dioxygenase Variant Rr41 (Bpdo-1.14.12.189.1e-5133.8438 *H
3gzxA, 3gzyAThe Biphenyl Dioxygenase In Complex With1.14.12.181.1e-5032.9444 *H
2b1xA, 2b1xC, 2b1xE, 2b24A, 2b24C, 2b24ENaphthalene 1,2-dioxygenase From Rhodoco1.2e-4434.2418 *H
3n0qAA Putative Aromatic-Ring Hydroxylating D1.6e-2029.2353 *H
3vcaA, 3vcpAQuaternary Ammonium Oxidative Demethylat1.5e-1828.0357 *H
3gkqA, 3gkqB, 3gkqC, 3gkqD, 3gkqE, 3gkqFTerminal Oxygenase Of Carbazole 1,9a-Dio0.0001225.6293 *H
1ww9A, 2de5A, 2de5B, 2de5C, 2de6A, 2de6B, 2de6C, 2de7A, 2de7B, 2de7C, 3vmgA, 3vmgB, 3vmgC, 3vmhA, 3vmhB, 3vmhC, 3vmiA, 3vmiB, 3vmiCThe Terminal Oxygenase Component Of Carb0.0003623.3417 *H

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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