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Proteins in PDB homologous to 2a84A

16 proteins (120 PDB structures) with E() < 0.001

Homologs in SwissProt


Acc   E.C. E() % id alen 44
&H
47
*H
196
&S
197
&S
198
&R
1mopA, 1mopB, 1n2bA, 1n2bB, 1n2eA, 1n2eB, 1n2gA, 1n2gB, 1n2hA, 1n2hB, 1n2iA, 1n2iB, 1n2jA, 1n2jB, 1n2oA, 1n2oB, 2a7xA, 2a84A, 2a86A, 2a86B, 2a88A, 3isjA, 3isjB, 3le8A, 3le8B, 4ef6A, 4ef6B, 4efkA, 4efkBA Pantothenate Synthetase From M. Tuberc6.3.2.11e-11596.5287 &H*H&S&S&R
3covA, 3covB, 3cowA, 3cowB, 3coyA, 3coyB, 3cozA, 3cozB, 3imcA, 3imcB, 3imeA, 3imeB, 3imgA, 3imgB, 3iobA, 3iobB, 3iocA, 3iocB, 3iodA, 3iodB, 3ioeA, 3ioeBMycobacterium Tuberculosis Pantothenate 6.3.2.11e-11596.5287 &H*H&S&S&R
3iubA, 3iubB, 3iueA, 3iueB, 3ivcA, 3ivcB, 3ivgA, 3ivgB, 3ivxA, 3ivxB, 4ddhA, 4ddhB, 4ddkA, 4ddkB, 4ddmA, 4ddmB, 4de5A, 4de5BPantothenate Synthetase From Mycobacteri6.3.2.11e-11596.5287 &H*H&S&S&R
1v8fA, 1v8fBPantoate-Beta-Alanine (Pantothenate Synt6.3.2.13e-4046.5271 &H*H&S&S&R
3innA, 3innB, 3innC, 3innDPantoate-Beta-Alanine-Ligase In Complex 6.3.2.14.1e-4044.6285 &H*H&S&S&R
1ufvA, 1ufvBPantothenate Synthetase From Thermus The6.3.2.11.7e-3845.4271 &H*H&S&S&R
3q10A, 3q10B, 3q10C, 3q10D, 3q12A, 3q12B, 3q12C, 3q12DPantoate-Beta-Alanine Ligase From Yersin6.3.2.13.9e-3844.1270 &H*H&S&S&R
1ihoA, 1ihoBCrystal Apo-Pantothenate Synthetase From6.3.2.16.3e-3843.5271 &H*H&S&S&R
3mueA, 3mueB, 3mueC, 3mueDPantoate-Beta-Alanine Ligase From Salmo 6.3.2.17.2e-3742.8271 &H*H&S&S&R
2x3fA, 2x3fBThe Methicillin-Resistant Staphylococcus6.3.2.11.5e-3538.6272 &H*H&S&S&R
3ag5A, 3ag5B, 3ag6A, 3ag6BPantothenate Synthetase From Staphylococ6.3.2.11.8e-3538.2272 &H*H&S&S&R
2ejcAPantoate--Beta-Alanine Ligase (Panc) Fro6.3.2.12.8e-3542.0264 &H*H&S&S&R
3uk2A, 3uk2BThe Pantothenate Synthetase From Burkhol3.2e-3441.5289 &H*H&S&S&R
3mxtA, 3uy4APantoate-Beta-Alanine Ligase From Campy 6.3.2.14.4e-3037.3255 &H*H&S&S&R
3n8hA, 3n8hB, 3qttA, 3qttBPantoate-Beta-Alanine Ligase From Franc 6.3.2.17e-2835.7258 &H*H&S&S&R
3guzA, 3guzBStructural And Substrate-Binding Studies6.3.2.12.4e-2748.2164 &H*H------

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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