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Proteins in PDB homologous to 1pknA

33 proteins (253 PDB structures) with E() < 0.001

Homologs in SwissProt


Acc   E.C. E() % id alen 72
&R
119
&R
269
&K
327
&T
1pknARabbit Muscle Pyruvate Kinase Complexed 2.7.1.40099.0519 &R&R&K&T
1aqfA, 1aqfB, 1aqfC, 1aqfD, 1aqfE, 1aqfF, 1aqfG, 1aqfH, 1a5uA, 1a5uB, 1a5uC, 1a5uD, 1a5uE, 1a5uF, 1a5uG, 1a5uH, 1a49A, 1a49B, 1a49C, 1a49D, 1a49E, 1a49F, 1a49G, 1a49HPyruvate Kinase From Rabbit Muscle With 2.7.1.403.1e-21797.9519 &R&R&K&T
1f3wA, 1f3wB, 1f3wC, 1f3wD, 1f3wE, 1f3wF, 1f3wG, 1f3wHRecombinant Rabbit Muscle Pyruvate Kinas2.7.1.405.7e-21797.7519 &R&R&K&T
1f3xA, 1f3xB, 1f3xC, 1f3xD, 1f3xE, 1f3xF, 1f3xG, 1f3xHS402p Mutant Of Rabbit Muscle Pyruvate K2.7.1.401.5e-21697.5519 &R&R&K&T
2g50A, 2g50B, 2g50C, 2g50D, 2g50E, 2g50F, 2g50G, 2g50HThe Location Of The Allosteric Amino Aci2.7.1.409.6e-21697.3519 &R&R&K&T
3n25A, 3n25B, 3n25C, 3n25D, 3n25E, 3n25F, 3n25G, 3n25HThe Muscle Pyruvate Kinase In Complex Wi2.7.1.409.6e-21697.3519 &R&R&K&T
3srfC, 3srfA, 3srfB, 3srfD, 3srfE, 3srfF, 3srfG, 3srfHHuman M1 Pyruvate Kinase9.9e-21395.6519 &R&R&K&T
1pkmAThe Refined Three-Dimensional Cat Muscle2.7.1.402.2e-21195.0519 &R&R&K&T
1zjhA, 4b2dA, 4b2dB, 4b2dCHuman Muscle Pyruvate Kinase (Pkm2)2.7.1.402e-20491.7519 &R&R&K&T
3gqyA, 3gqyB, 3gqyC, 3gqyD, 3gr4A, 3gr4B, 3gr4C, 3gr4D, 3h6oA, 3h6oB, 3h6oC, 3h6oD, 3me3A, 3me3B, 3me3C, 3me3DActivator-Bound Human Pyruvate Kinase M22.7.1.402e-20491.7519 &R&R&K&T
3srdA, 3srdB, 3srdC, 3srdD, 3srhA, 3srhB, 3srhC, 3srhDHuman M2 Pyruvate Kinase In Complex With2e-20491.7519 &R&R&K&T
3g2gA, 3g2gB, 3g2gC, 3g2gDS437y Mutant Of Human Muscle Pyruvate Ki2.7.1.405.6e-20491.5519 &R&R&K&T
3bjtA, 3bjtB, 3bjtC, 3bjtDPyruvate Kinase M2 Is A Phosphotyrosine 2.7.1.407.7e-20491.5519 &R&R&K&T
1t5aA, 1t5aB, 1t5aC, 1t5aDHuman Pyruvate Kinase M22.7.1.408.4e-20491.5519 &R&R&K&T
3bjfA, 3bjfB, 3bjfC, 3bjfDPyruvate Kinase M2 Is A Phosphotyrosine 2.7.1.401.6e-20391.5518 &R&R&K&T
2vgbA, 2vgbB, 2vgbC, 2vgbDHuman Erythrocyte Pyruvate Kinase2.7.1.401.1e-15568.5517 &R&R&K&T
2vgfA, 2vgfB, 2vgfC, 2vgfDHuman Erythrocyte Pyruvate Kinase: T384m2.7.1.402.8e-15568.3517 &R&R&K&T
2vggA, 2vggB, 2vggC, 2vggDHuman Erythrocyte Pyruvate Kinase: R479h2.7.1.403.3e-15568.3517 &R&R&K&T
2vgiA, 2vgiB, 2vgiC, 2vgiDHuman Erythrocyte Pyruvate Kinase: R486w2.7.1.405.2e-15568.3517 &R&R&K&T
1a3wA, 1a3wB, 1a3xA, 1a3xBPyruvate Kinase From Saccharomyces Cerev2.7.1.401.4e-9849.6506 &R&R&K&T
3e0vA, 3e0vB, 3e0vC, 3e0vD, 3e0vE, 3e0vF, 3e0wAPyruvate Kinase From Leishmania Mexicana2.7.1.401.9e-9348.2506 &R&R&K&T
3pp7A, 3pp7BLeishmania Mexicana Pyruvate Kinase In C2.7.1.404.4e-9348.3505 &R&R&K&T
1pklA, 1pklB, 1pklC, 1pklD, 1pklE, 1pklF, 1pklH, 1pklG, 3ktxA, 3ktxB, 3hqnD, 3hqnA, 3hqoK, 3hqoA, 3hqoB, 3hqoC, 3hqpA, 3hqpB, 3hqpC, 3hqpD, 3hqpE, 3hqpF, 3hqpG, 3hqpH, 3hqpI, 3hqpJ, 3hqpK, 3hqpL, 3hqpM, 3hqpN, 3hqpO, 3hqpP, 3hqqA, 3hqqB, 3hqqC, 3hqqD, 3hqqE, 3hqqF, 3hqqG, 3hqqH, 3hqqI, 3hqqJ, 3hqqK, 3hqqL, 3hqqM, 3hqqN, 3hqqO, 3hqqP, 3hqqQ, 3hqqR, 3hqqS, 3hqqT, 3hqqU, 3hqqV, 3hqqW, 3hqqX, 3is4A, 3is4B, 3qv6A, 3qv6D, 3qv7D, 3qv7A, 3qv7B, 3qv7C, 3qv8D, 3qv8A, 3srkA, 3srkBThe Leishmania Pyruvate Kinase2.7.1.404.4e-9348.3505 &R&R&K&T
3qv9A, 3qv9BTrypanosoma Cruzi Pyruvate Kinase(Tcpyk)2.5e-9249.0506 &R&R&K&T
2e28ACrystal Structure Analysis Of Pyruvate K2.7.1.402.3e-8145.9492 &R&R&K&T
3khdA, 3khdB, 3khdC, 3khdDPff1300w.9.5e-8143.3503 &R&R&K&T
3eoeA, 3eoeB, 3eoeC, 3eoeD, 3gg8A, 3gg8B, 3gg8C, 3gg8DPyruvate Kinase From Toxoplasma Gondii, 3.8e-8043.3496 &R&R&K&T
3t05A, 3t05B, 3t05C, 3t05D, 3t07A, 3t07B, 3t07C, 3t07D, 3t0tA, 3t0tB, 3t0tC, 3t0tDS. Aureus Pyruvate Kinase2.7.1.402e-7944.5488 &R&R&K&T
1pkyA, 1pkyB, 1pkyC, 1pkyDPyruvate Kinase From E. Coli In The T-St2.7.1.407.8e-7946.3486 &R&R&K&T
1e0uA, 1e0uB, 1e0uC, 1e0uDStructure R271l Mutant Of E. Coli Pyruva2.7.1.409.1e-7946.3486 &R&R&K&T
1e0tA, 1e0tB, 1e0tC, 1e0tDR292d Mutant Of E. Coli Pyruvate Kinase2.7.1.403.2e-7846.1486 &R&R&K&T
3ma8A, 3ma8BCgd1_2040, A Pyruvate Kinase From Crypto1.8e-7742.2516 &R&R&K&T
3qtgA, 3qtgBPyruvate Kinase From Pyrobaculum Aerophi2.7.1.407.2e-3329.3478 &R&R&K&T

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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