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Proteins in PDB homologous to 1j09A

23 proteins (70 PDB structures) with E() < 0.001

Homologs in SwissProt


Acc   E.C. E() % id alen 246
&K
1j09A, 1n75A, 1n77A, 1n77B, 1n78A, 1n78B, 2cuzA, 2cv0A, 2cv0B, 2cv1A, 2cv1B, 2cv2A, 2cv2B, 2dxiA, 2dxiBThermus Thermophilus Glutamyl-Trna Synth6.1.1.172.3e-199100.0468 &K
1g59A, 1g59C, 1glnAGlutamyl-Trna Synthetase Complexed With 6.1.1.171.6e-19799.4468 &K
2o5rAGlutamyl-Trna Synthetase 1 (Ec 6.1.1.17)6.1.1.173.5e-7042.5475 &K
4griA, 4griBA Glutamyl-Trna Synthetase Glurs From Bo3.2e-6940.0485 &K
3akzB, 3akzD, 3akzC, 3akzAThermotoga Maritima Nondiscriminating Gl6.1.1.171.9e-6841.6474 &K
3afhAThermotoga Maritima Nondiscriminating Gl6.1.1.171.9e-6841.6474 &K
3al0CThe Glutamine Transamidosome From Thermo6.1.1.172.4e-6841.6474 &K
2cfoA, 2cfoBNon-discriminating Glutamyl-trna Synthet6.1.1.172e-5839.5473 &K
3pnvA, 3pnvBV369m Mutant Of Glutamyl-Trna Synthetase2.6e-5637.5483 &K
2ja2AMycobacterium Tuberculosis Glutamyl-Trna6.1.1.176.4e-5637.3483 &K
3pnyA, 3pnyBGlutamyl-Trna Synthetase From Mycobacter6.6e-5637.3483 &K
4g6zAA Glutamyl-Trna Synthetase Glurs From Bu1.2e-5135.2477 &K
1nzjA, 4a91ACrystal Structure And Activity Studies O4.3e-2434.0294 &K
3aiiAArchaeal Non-Discriminating Glutamyl-Trn6.1.1.173.6e-2128.7443 &R
2hz7AThe Glutaminyl-Trna Synthetase From Dein6.1.1.181.1e-1129.9308 &K
2rd2A, 2re8AGlutaminyl-Trna Synthetase Mutant C229r 6.1.1.183.9e-0624.3411 &K
1nylAUnliganded Glutaminyl-Trna Synthetase6.1.1.185.9e-0624.4422 &K
1euqA, 1euyA, 1exdAGlutaminyl-Trna Synthetase Complexed Wit6.1.1.186e-0624.4422 &K
1gsgP, 1gtrA, 1gtsA, 1qtqA, 1zjwA, 4jxxA, 4jxzAE.Coli Glutaminyl-Trna Synthetase Comple6.1.1.186.1e-0624.4422 &K
1o0bA, 1o0cAL-Glutamine And Ampcpp Bound To Glutamin6.1.1.186.1e-0624.4422 &K
1qrtAGlutaminyl-Trna Synthetase Mutant D235g 6.1.1.188.3e-0624.2422 &K
1qrsAGlutaminyl-Trna Synthetase Mutant D235n 6.1.1.188.3e-0624.2422 &K
1qruAGlutaminyl-Trna Synthetase Mutant I129t 6.1.1.181.5e-0524.2422 &K

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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