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Proteins in PDB homologous to 1q6lA

Additional 1q6l chains
1q6lB

71 proteins (258 PDB structures) with E() < 0.001

Homologs in SwissProt


Acc   E.C. E() % id alen 64
&K
112
&E
136
*H
1kv8A, 1kv8B, 1kw1A, 1kw1B, 1q6lA, 1q6lB, 1q6oA, 1q6oB, 1q6qA, 1q6qB, 1q6rA, 1q6rB, 1xbvA, 1xbvB3-Keto-L-Gulonate 6-Phosphate Decarboxyl4.1.1.853.8e-93100.0214 &K&E*H
1so5A, 1so5BE112q Mutant Of 3-keto-l-gulonate 6- Pho4.1.1.857.4e-9399.5214 &K&Q*H
1so4A, 1so4BK64a Mutant Of 3-Keto-L-Gulonate 6- Phos4.1.1.851.2e-9299.5214 &A&E*H
1xbyA, 1xbyB3-Keto-L-Gulonate 6-Phosphate Decarboxyl4.1.1.851.7e-9299.1214 &K&D*H
1so3A, 1so3BH136a Mutant Of 3-Keto-L-Gulonate 6- Pho4.1.1.852.7e-9299.5214 &K&E*A
1so6A, 1so6BE112qH136A DOUBLE MUTANT OF 3-Keto-L- Gu4.1.1.855.2e-9299.1214 &K&Q*A
1xbxA, 1xbxB, 1xbzA, 1xbzB3-Keto-L-Gulonate 6-Phosphate Decarboxyl4.1.1.858.6e-9298.6214 &K&D*H
3exrA, 3exrB, 3exrC, 3exrD, 3exsA, 3exsB, 3exsC, 3exsD, 3extAKgpdc From Streptococcus Mutans3.4e-4146.8216 &K&E*H
3iebA, 3iebB, 3iebC, 3iebD, 3iebE, 3jr2A, 3jr2B, 3jr2C, 3jr2D3-Keto-L-Gulonate-6-Phosphate Decarboxyl5.9e-3643.4212 &K&E*H
3f4wA, 3f4wBThe 1.65a 3-Hexulose-6-Phosphate Synthas2.6e-1834.1205 &K&D*H
3ajxA, 3ajxB, 3ajxC, 3ajxD3-Hexulose-6-Phosphate Synthase4.1.2.434.9e-1835.1208 &K&D*H
3lv6A, 3lv6BThe Mutant I218f Of Orotidine 5'-Monoph 4.1.1.234.5e-0526.6222 &K&E*P
3nq7A, 3nq7BThe Mutant F71a Of Orotidine 5'-Monophos4.1.1.234.5e-0526.6222 &K&E*P
3lhuA, 3lhuBThe Mutant I199f Of Orotidine 5'-Monoph 4.1.1.235.3e-0524.8218 &K--*E
3nqdA, 3nqdB, 3pbvA, 3pbvBThe Mutant I96t Of Orotidine 5'-Monophos4.1.1.236.2e-0526.6222 &K&E*P
3p61A, 3p61BThe Mutant R160a Of Orotidine 5'-Monopho4.1.1.236.2e-0524.8218 &K--*E
3lhzA, 3lhzB, 3m44A, 3m44BThe Mutant V201a Of Orotidine 5'-Monoph 4.1.1.237.3e-0526.6222 &K&E*P
3qmrA, 3qmrBThe Mutant R160a,V182a Of Orotidine 5'- 7.3e-0525.1219 &K--*E
3sj3A, 3sj3BThe Mutant R160a.Y206f Of Orotidine 5'- 4.1.1.238.6e-0524.8218 &K--*E
3nqgA, 3nqgBThe Mutant V155d Of Orotidine 5'-Monopho4.1.1.238.6e-0524.3218 &K--*E
3nqcA, 3nqcB, 3pbuA, 3pbuBThe Mutant I96s Of Orotidine 5'-Monophos4.1.1.230.000126.1222 &K&E*P
3m1zA, 3m1zB, 3m5yA, 3m5yBThe Mutant V182a.V201a Of Orotidine 5'- 4.1.1.230.000125.1219 &K--*E
3sizA, 3sizB, 3sy5A, 3sy5BThe Mutant S127a Of Orotidine 5'-Monopho4.1.1.230.000124.8218 &K--*E
3p5zA, 3p5zBThe Mutant T159s Of Orotidine 5'-Monopho4.1.1.230.000126.6222 &K&E*P
1km1A, 1km1BOrotidine Monophosphate Decarboxylase Mu4.1.1.230.0001124.8218 &K--*E
3nq6A, 3nq6BThe Mutant P180a Of Orotidine 5'-Monopho4.1.1.230.0001226.1222 &K&E*P
3nqfA, 3nqfB, 3pbyA, 3pbyBThe Mutant L123s Of Orotidine 5'-Monopho4.1.1.230.0001224.3218 &K--*E
1loqAOrotidine Monophosphate Decarboxylase Co4.1.1.230.0001226.1222 &K&E*P
3p5yA, 3p5yBThe Mutant T159a Of Orotidine 5'-Monopho4.1.1.230.0001224.5220 &K&F*R
3sguAMethanothermobacter Thermautotrophicus O0.0001326.1222 &K&E*P
3nqaA, 3nqaBThe Mutant F100a Of Orotidine 5'-Monopho4.1.1.230.0001426.1222 &K&E*P
3nqmA, 3nqmB, 3pc0A, 3pc0BThe Mutant V155s Of Orotidine 5'-Monopho4.1.1.230.0001424.3218 &K--*E
3nqeA, 3nqeB, 3pbwA, 3pbwBThe Mutant L123n Of Orotidine 5'-Monopho4.1.1.230.0001426.1222 &K&E*P
1km2AOrotidine Monophosphate Mutant Q185a Wit4.1.1.230.0001626.1222 &K&E*P
1dv7AOrotidine Monophosphate Decarboxylase4.1.1.230.0001626.1222 &K&E*P
3lldA, 3lldBThe Mutant S127g Of Orotidine 5'-Monoph 4.1.1.230.0001724.4221 &K&T*R
3llfA, 3llfBThe Mutant S127p Of Orotidine 5'-Monoph 4.1.1.230.0001725.7222 &K&P*P
3lhvA, 3lhvB, 3lhvC, 3lhvDThe Mutant V182a.I199a.V201a Of Orotidi 4.1.1.230.0001724.8218 &K--*E
3g18A, 3g18B, 3g1aA, 3g1aB, 3g1dA, 3g1dB, 3g1fA, 3g1fB, 3g1fC, 3g1fD, 3g1fE, 3g1fF, 3g1fG, 3g1fH, 3g1fI, 3g1fJ, 3g1fK, 3g1fL, 3g1fM, 3g1hA, 3g1hB, 3g1hC, 3g1hD, 3g1hE, 3g1hF, 3g1hG, 3g1hH, 3g1hI, 3g1hJ, 3g1hK, 3g1hL, 3g1hM, 3ltpA, 3ltpBOrotidine 5'-Monophosphate Decarboxylase4.1.1.230.0001726.1222 &K&E*P
1lorAOrotidine 5'-Monophosphate Complexed Wit4.1.1.230.0001726.1222 &K&E*P
1lolA, 1lolB, 1lp6A, 1lp6BOrotidine Monophosphate Decarboxylase Co4.1.1.230.0001726.1222 &K&E*P
1dvjA, 1dvjB, 1dvjC, 1dvjDOrotidine Monophosphate Decarboxylase Co4.1.1.230.0001826.1222 &K&E*P
3secA, 3ssjA, 3sw6A, 3thqA, 3thqBMethanothermobacter Thermautotrophicus O0.0001826.1222 &K&E*P
1x1zA, 1x1zB, 2e6yA, 2e6yB, 2zz1A, 2zz1B, 2zz6A, 2zz6B, 3w07AOrotidine 5'-Monophosphate Decarboxylase4.1.1.230.0001926.1222 &K&E*P
3lhyA, 3lhyB, 3m43A, 3m43BThe Mutant I199a Of Orotidine 5'-Monoph 4.1.1.230.0002324.3218 &K--*E
3rlvA, 3rlvBThe Mutant Y206f Of Orotidine 5'-Monopho0.0002326.1222 &K&E*P
3lhwA, 3lhwB, 3m41A, 3m41BThe Mutant V182a Of Orotidine 5'-Monoph 4.1.1.230.0002324.7219 &K--*E
3lv5A, 3lv5BThe Mutant I199e Of Orotidine 5'-Monoph 4.1.1.230.0002324.3218 &K--*E
1km3AOdcase Mutant K42a Complexed With 6-azau4.1.1.230.0002526.1222 &K&E*P
3li1A, 3li1B, 3m47A, 3m47BThe Mutant I218a Of Orotidine 5'-Monoph 4.1.1.230.0002726.1222 &K&E*P
3p60A, 3p60BThe Mutant T159v Of Orotidine 5'-Monopho4.1.1.230.0002724.1220 &K&F*R
3qezA, 3qezBThe Mutant T159v,V182a Of Orotidine 5'- 0.0002723.6216 &K&F*R
3lhtA, 3lhtBThe Mutant V201f Of Orotidine 5'-Monoph 4.1.1.230.0002726.1222 &K&E*P
3rluA, 3rluBThe Mutant K82a Of Orotidine 5'-Monophos0.0003226.1222 &K&E*P
3qmtA, 3qmtBThe Mutant V182a,Y206f Of Orotidine 5'- 0.0003224.7219 &K--*E
3ltyA, 3ltyB, 3m5zA, 3m5zBThe Mutant V182a,I218a Of Orotidine 5'- 4.1.1.230.0003724.7219 &K--*E
3qf0A, 3qf0BThe Mutant T159v,Y206f Of Orotidine 5'- 0.0003724.1220 &K&F*R
3ltsA, 3ltsB, 3m5xA, 3m5xBThe Mutant V182a,I199a Of Orotidine 5'- 4.1.1.230.0003724.3218 &K--*E
3qmsA, 3qmsBThe Mutant T159v,V182a,Y206f Of Orotidin0.0003723.6216 &K&F*R
1losA, 1losB, 1losC, 1losDOrotidine Monophosphate Decarboxylase Mu4.1.1.230.0004327.1107 &K----
3g1yA, 3g1yB, 3g22A, 3g22B, 3g24A, 3g24BThe Mutant D70n Of Orotidine 5'- Monopho4.1.1.230.0004425.7222 &K&E*P
3li0A, 3li0BThe Mutant R203a Of Orotidine 5'-Monoph 4.1.1.230.0004427.1107 &K----
1km0A, 1km0B, 1km0C, 1km0DOrotidine Monophosphate Decarboxylase Mu4.1.1.230.0004925.7222 &K&E*P
1km5AOdcase Mutant D75n Complexed With 6-Azau4.1.1.230.0004925.7222 &K&E*P
2zz4A, 2zz4BCovalent Complex Of Orotidine Monophosph4.1.1.230.000525.7222 &K&E*P
1km4AOdcase Mutant K72a Complexed With Ump4.1.1.230.0005725.7222 &A&E*P
2zz2A, 2zz2B, 2zz7AOrotidine Monophosphate Decarboxylase K74.1.1.230.0005925.7222 &A&E*P
3g1sA, 3g1sB, 3g1vA, 3g1vB, 3g1xA, 3g1xBThe Mutant D70g Of Orotidine 5'- Monopho4.1.1.230.0007225.7222 &K&E*P
1klyAOrotidine Monophosphate Decarboxylase D74.1.1.230.0007925.7222 &K&E*P
1klzAOrotidine Monophosphate Decarboxylase Mu4.1.1.230.0009425.7222 &K&E*P
2zz3A, 2zz3BCovalent Complex Of Orotidine Monophosph4.1.1.230.0009625.7222 &K&E*P

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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