Proteins in PDB homologous to 1b6tA

16 proteins (91 PDB structures) with E() < 0.001

Homologs in SwissProt

Acc   E.C. E() % id alen 18
1qjcA, 1qjcBPhosphopantetheine Adenylytransferase Fr2.7.7.33e-73100.0157 &H&K&R%S
1b6tA, 1b6tB, 1gn8A, 1gn8B, 1h1tA, 1h1tBPhosphopantetheine Adenylyltransferase I2. &H&K&R%S
3l92A, 3l93APhosphopantetheine Adenylyltransferase F2. &H&K&R%S
1od6AThe Phosphopantetheine Adenylyltransfera2. &H&K&R%S
3pxuAPhosphopantetheine Adenylyltransferase F2. &H&K&R%G
3k9wAPhosphopantetheine Adenylyltransferase F2. &H&K&R%G
3otwA, 3otwB, 3otwC, 3otwD, 3otwE, 3otwFStructural And Functional Studies Of Hel2. &H&K&R%S
3nv7AH.Pylori Phosphopantetheine Adenylyltran2. &H&K&R%S
1vlhA, 1vlhB, 1vlhC, 1vlhD, 1vlhE, 1vlhFPhosphopantetheine Adenylyltransferase ( &H&K&R%S
3f3mASix Crystal Structures Of Two Phosphopan2. &H&K&R%S
3nd5A, 3nd5B, 3nd5C, 3nd5D, 3nd5E, 3nd5F, 3nd6A, 3nd6B, 3nd6C, 3nd6D, 3nd6E, 3nd6F, 3nd7A, 3nd7B, 3nd7C, 3nd7D, 3nd7E, 3nd7FPhosphopantetheine Adenylyltransferase ( &H&K&R%S
4f3rA, 4f3rB, 4f3rCPhosphopantetheine Adenylyltransferase (1.8e-2945.5154 &H&K&R%G
1tfuA, 3rbaA, 3rffA, 3rhsA, 3uc5APhosphopantetheine Adenylyltransferase F2. &H&K&R%S
3lcjA, 4e1aAPhosphopantetheine Adenylyltransferase F2. &H&K&R%S
3nbaA, 3nbaB, 3nbaC, 3nbaD, 3nbkA, 3nbkB, 3nbkC, 3nbkD, 3pnbA, 3pnbB, 3pnbC, 3pnbDPhosphopantetheine Adenylyltranferase Fr2.7.7.33e-2945.2155 &H&K&R%S
1o6bAPhosphopantetheine Adenylyltransferase W2. &H&K&R%S

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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