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Proteins in PDB homologous to 1p5dX

20 proteins (45 PDB structures) with E() < 0.001

Homologs in SwissProt


Acc   E.C. E() % id alen 20
&R
108
#S
109
&H
118
&K
247
&R
329
&H
1k2yXPhosphomannomutase/phosphoglucomutase S15.4.2.2, 5.4.2.85.9e-19999.8455 &R#A&H&K&R&H
2fkmXPmm/pgm S108d Mutant With Alpha-d-glucos5.4.2.2, 5.4.2.86.9e-19999.8455 &R#D&H&K&R&H
2fkfAPhosphomannomutasePHOSPHOGLUCOMUTASE FRO5.4.2.2, 5.4.2.88.1e-19999.8455 &R#X&H&K&R&H
2h4lX, 2h5aXComplex Of PmmPGM WITH RIBOSE 1-Phosphat5.4.2.2, 5.4.2.88.1e-19999.8455 &R#X&H&K&R&H
3rsmAS108c Mutant Of PmmPGM8.1e-19999.8455 &R#C&H&K&R&H
1p5dX, 1p5gX, 1pcjX, 1pcmXEnzyme-Ligand Complex Of P. Aeruginosa P5.4.2.2, 5.4.2.88.1e-19999.8455 &R#X&H&K&R&H
3bkqX, 3c04AThe P368g Mutant Of PmmPGM IN COMPLEX WI5.4.2.2, 5.4.2.85.4e-19899.6455 &R#X&H&K&R&H
1k35APhosphomannomutase/phosphoglucomutase Fr5.4.2.2, 5.4.2.81.9e-19498.0455 &R#X&H&K&R&H
3uw2AX-Ray PhosphoglucomutasePHOSPHOMANNOMUTA4.7e-11056.0461 &R#S&H&K&R&H
1wqaA, 1wqaB, 1wqaC, 1wqaDPyrococcus Horikoshii Phosphomannomutase3.3e-4632.4441 &R#S&H&K&R&G
2f7lA, 2f7lBSulfolobus Tokodaii PhosphomannomutasePH1.6e-3028.9461 &R#S&H&K&R&G
3pdkA, 3pdkBPhosphoglucosamine Mutase From B. Anthra5.4.2.101.6e-2829.6463 &R#S&H&K&R&H
1tuoAPutative Phosphomannomutase From Thermus6.8e-2228.0439 &R#S&H&K&R&G
3i3wA, 3i3wBA Phosphoglucosamine Mutase From Francis5.4.2.102.4e-2030.4448 &R#X&H&K&R&H
1lxtA, 1lxtB, 1c47A, 1c47B, 1c4gA, 1c4gBPhosphotransferase Phosphoglucomutase Fr5.4.2.23.3e-1024.8379 --#S&H&N&R&H
1jdyA, 1jdyB, 1vklA, 1vklB, 3pmgA, 3pmgBRabbit Muscle Phosphoglucomutase5.4.2.28.5e-1024.5379 --#X&H&N&R&H
2z0fA, 2z0fBPutative Phosphoglucomutase From Thermus4.7e-0824.3419 --#S&H&K&R&A
3na5A, 3na5BA Bacterial Phosphoglucomutase, An Enzym1.4e-0622.6482 &R#S&H&K&R&A
3olpA, 3olpBA Bacterial Phosphoglucomutase, An Enzym2.3e-0622.6482 &R#S&H&K&R&A
2fuvA, 2fuvBPhosphoglucomutase From Salmonella Typhi1.5e-0522.1484 &R#S&H&K&R&A

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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