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Proteins in PDB homologous to 1gpmB

17 proteins (63 PDB structures) with E() < 0.001

Homologs in SwissProt


Acc   E.C. E() % id alen 59
%G
86
*C
87
%Y
181
*H
183
&E
239
&D
381
&K
1gpmA, 1gpmB, 1gpmC, 1gpmDEscherichia Coli Gmp Synthetase Complexe6.3.5.2095.4523 %G*C%Y*H&E&D&K
3tqiA, 3tqiB, 3tqiC, 3tqiDThe Gmp Synthase (Guaa) From Coxiella Bu6.3.5.26.7e-15059.1523 %G*C%Y*H&E&D&K
2ywbA, 2ywbB, 2ywbC, 2ywbDGmp Synthetase From Thermus Thermophilus6.3.5.22.4e-10247.9516 %G*C%Y*H&E&D&K
2ywcA, 2ywcB, 2ywcC, 2ywcDGmp Synthetase From Thermus Thermophilus6.3.5.25e-10047.1516 %G*C%Y*H&E&D&K
3uowA, 3uowBPf10_0123, A Gmp Synthetase From Plasmod1.9e-9440.3549 %G*C%Y*H&E&D&K
2dplA, 2dplB, 3a4iA, 3a4iBThe Gmp Synthase From Pyrococcus Horikos6.3.5.21.7e-5847.8318 ----------&D&K
2vxoA, 2vxoBHuman Gmp Synthetase In Complex With Xmp6.3.5.22.8e-5735.0569 %G*C%Y*H&E&D&K
2d7jACrystal Structure Analysis Of Glutamine 6.3.5.21.8e-2434.7193 %G*C%L*H&E----
2vpiA, 2vpiBHuman Gmp Synthetase - Glutaminase Domai6.3.5.23.8e-2437.5200 %G*C%Y*H&E----
1wl8APh1346 Protein From Pyrococcus Horikoshi6.3.5.22.3e-2334.2193 %G*C%L*H&E----
2a9vA, 2a9vB, 2a9vC, 2a9vDA Putative Gmp Synthase Subunit A Protei6.3.5.26.3e-1929.5207 %G*C%V*H&E----
1i7qB, 1i7qD, 1i7sB, 1i7sDAnthranilate Synthase From S. Marcescens4.1.3.271.1e-0626.6192 %G*C%L*H&E----
1qdlBThe Anthranilate Synthase From Sulfolobu4.1.3.271.5e-0626.3198 %G*C%L*H&E----
1i1qBThe Cooperative Allosteric Anthranilate 2.4.2.18, 4.1.3.274.3e-0525.8194 %G*C%L*H&E----
1t36B, 1t36D, 1t36F, 1t36HE. Coli Carbamoyl Phosphate Synthetase S6.3.5.50.0004222.5200 %G*C%L*H&E----
1m6vB, 1m6vD, 1m6vF, 1m6vHThe G359f (Small Subunit) Point Mutant O6.3.5.50.0008322.5200 %G*C%L*H&E----
1jdbC, 1jdbF, 1jdbI, 1jdbL, 1bxrB, 1bxrD, 1bxrF, 1bxrH, 1ce8B, 1ce8D, 1ce8F, 1ce8HCarbamoyl Phosphate Synthetase From Esch6.3.5.50.0009822.5200 %G*C%L*H&E----

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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