Proteins in PDB homologous to 2qf7A

39 proteins (134 PDB structures) with E() < 0.001

Homologs in SwissProt

Acc   E.C. E() % id alen 549
2qf7A, 2qf7BA Complete Multifunctional Pyruvate Carb093.31152 *D&D*X
3tw7A, 3tw7B, 3tw6A, 3tw6B, 3tw6C, 3tw6DRhizobium Etli Pyruvate Carboxylase T882093.21152 *D&D*X
3ho8A, 3ho8D, 3ho8C, 3ho8BS. Aureus Pyruvate Carboxylase In Comple047.51150 *D&D*K
3bg5A, 3bg5B, 3bg5C, 3bg5DStaphylococcus Aureus Pyruvate Carboxyla047.51150 *D&D*K
3hblA, 3hblB, 3hblC, 3hblDS. Aureus Pyruvate Carboxylase T908a Mut047.41150 *D&D*K
3hb9A, 3hb9B, 3hb9C, 3hb9DS. Aureus Pyruvate Carboxylase A610t Mut047.41150 *D&D*K
3bg3A, 3bg3B, 3bg3C, 3bg3DHuman Pyruvate Carboxylase (Missing The *D&D*X
3bg9A, 3bg9B, 3bg9C, 3bg9DHuman Pyruvate Carboxylase (Missing The *D&D*K
2dzdA, 2dzdBThe Biotin Carboxylase Domain Of Pyruvat6.8e-8748.5462 ------
1ulzAThe Biotin Carboxylase Subunit Of Pyruva8.2e-6238.2463 ------
2vpqA, 2vpqBBiotin Carboxylase From S. Aureus Comple1.5e-5936.8456 ------
2nx9A, 2nx9BThe Carboxyltransferase Domain Of The Ox8.3e-5937.5440 *D&D*K
3u9sA, 3u9sC, 3u9sE, 3u9sG, 3u9sI, 3u9sK, 3u9tAP. Aeruginosa 3-methylcrotonyl-coa Carbo4.9e-5838.8459 ------
3n6rA, 3n6rC, 3n6rE, 3n6rG, 3n6rI, 3n6rKThe Holoenzyme Of Propionyl-coa Carboxyl4.9e-5736.1485 ------
3g8cA, 3g8cBCrystal Stucture Of Biotin Carboxylase I6.3.4.14, ------
1bncA, 1bncB, 1dv1A, 1dv1B, 2j9gA, 2j9gB, 2vr1A, 2vr1B, 2v58A, 2v58B, 2v59A, 2v59B, 2v5aA, 2v5aB, 2w6mA, 2w6mB, 2w6nA, 2w6nB, 2w6oA, 2w6oC, 2w6pA, 2w6pB, 2w6qA, 2w6qB, 2w6zA, 2w6zB, 2w70A, 2w70B, 2w71A, 2w71C, 4hr7A, 4hr7C, 4hr7E, 4hr7FThree-Dimensional The Biotin Carboxylase6.3.4.14, ------
3rupA, 3rupB, 3rv3A, 3rv3BE.Coli Biotin Carboxylase In Complex Wit6.3.4.14, ------
3jzfA, 3jzfB, 3jziA, 3jziBBiotin Carboxylase From E. Coli In Compl6.3.4.14, ------
1dv2A, 1dv2BThe Biotin Carboxylase, Mutant E288k, Co6.3.4.14, ------
2gpsA, 2gpsBThe Biotin Carboxylase Subunit, E23r Mut6.3.4.14, ------
3g8dA, 3g8dBThe Biotin Carboxylase Subunit, E296a Mu6.3.4.14, ------
3rv4AE.Coli Biotin Carboxylase R16e Mutant In6.3.4.14, ------
2gpwA, 2gpwB, 2gpwC, 2gpwDThe Biotin Carboxylase Subunit, F363a Mu6.3.4.14, ------
2vqdA, 2c00A, 2c00BBiotin Carboxylase From Pseudomonas Aeru6.3.4.14, ------
3ouzA, 3ouzB, 3ouuA, 3ouuBBiotin Carboxylase-Adp Complex From Camp1.8e-5136.0455 ------
1rqeAPropionibacterium Shermanii Transcarboxy2. *D&D*K
1u5jAPropionibacterium Shermanii Transcarboxy2. *D&D*X
1s3hAPropionibacterium Shermanii Transcarboxy2. *D&D*X
1rqhAPropionibacterium Shermanii Transcarboxy2. *D&D*K
1rr2APropionibacterium Shermanii Transcarboxy2. *D&D*K
3va7AThe Kluyveromyces Lactis Urea Carboxylas5e-4732.9459 ------
1rqbAPropionibacterium Shermanii Transcarboxy2.1.3.19e-4532.8509 *D&D*X
1w93ABiotin Carboxylase Domain Of Acetyl- Coe6.3.4.14, ------
1w96A, 1w96B, 1w96CBiotin Carboxylase Domain Of Acetyl- Coe6.3.4.14, ------
2hjwAThe Bc Domain Of Acc26.3.4.14, ------
3jrwAPhosphorylated Bc Domain Of Acc26.3.4.14, ------
3jrxAThe Bc Domain Of Acc2 In Complex With So6.3.4.14, ------
2yl2A, 2yl2BHuman Acetyl-Coa Carboxylase 1, Biotin C6.3.4.14, ------
3gidA, 3gidB, 3glkAThe Biotin Carboxylase (Bc) Domain Of Hu6.3.4.14, ------

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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