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Proteins in PDB homologous to 1wpoA

20 proteins (47 PDB structures) with E() < 0.001

Homologs in SwissProt


Acc   E.C. E() % id alen 63
*H
132
*S
134
&S
157
&H
165
%R
166
&R
1njtA, 1njtB, 1njtC, 1njtD, 1njuA, 1njuB, 1njuC, 1njuD, 1nkmA, 1nkmBComplex Hcmv Protease And A Peptidomimet3.4.21.971.4e-11682.3248 *H*S&S&H%R&R
1nkkA, 1nkkB, 1nkkC, 1nkkDComplex Hcmv Protease And A Peptidomimet3.4.21.971.4e-11682.3248 *H*S&S&H%R&R
1layACytomegalovirus Protease3.4.21.971.4e-11682.3248 *H*S&S&H%R&R
1wpoA, 1wpoBHydrolytic Enzyme Human Cytomegalovirus 3.4.21.971.7e-11683.5248 *H*S&S&H%R&R
2wpoA, 2wpoB, 2wpoC, 2wpoDHcmv Protease Inhibitor Complex3.4.21.971.7e-11682.3248 *H*S&S&H%R&R
1cmvA, 1cmvBHuman Cytomegalovirus Protease3.4.21.971.7e-11682.3248 *H*S&S&H%R&R
1iefA, 1iefBThe Catalytic Site Mutant S134a Of The H3.4.21.973.3e-11681.9248 *H*S&A&H%R&R
1jq7A, 1jq7BHcmv Protease Dimer-Interface Mutant, S23.4.21.976.3e-11681.9248 *H*S&S&H%R&R
1id4A, 1id4BThe Catalytic Site Mutant (H157q) Of The3.4.21.979.7e-11681.9248 *H*S&S&Q%R&R
1iedA, 1iedBThe Catalytic Site Mutant (H157e) Of The3.4.21.971.2e-11581.9248 *H*S&S&E%R&R
1iegA, 1iegBThe Catalytic Site Mutant S134aH157A OF 3.4.21.974.4e-11581.5248 *H*S&A&A%R&R
1iecA, 1iecBThe Catalytic Site Mutant (H157a) Of The3.4.21.976.8e-11581.5248 *H*X&S&A%R&R
1jq6AHuman Cytomegalovirus Protease Dimer-Int3.4.21.973.3e-11381.5248 *H*S&S&H%R&R
2pbkA, 2pbkBKshv Protease In Complex With Hexapeptid4.4e-2732.4244 *H*S&S&H%R&R
1fl1A, 1fl1BKshv Protease4.4e-2732.4244 *H*S&S&H%R&R
3njqBKaposi's Sarcoma-Associated Herpesvirus 9.1e-2335.2179 *H*S&S&H%R&R
3njqAKaposi's Sarcoma-Associated Herpesvirus 9.1e-2335.2179 *H*S&S&H%R&R
1o6eA, 1o6eBEpstein-Barr Virus Protease3.4.21.971.8e-1929.4248 *H*S&A&H%R&R
1at3A, 1at3BHerpes Simplex Virus Type Ii Protease6.5e-1424.5245 *H*S&S&H%R&R
1vzvAVaricella-Zoster Virus Protease3.4.21.974.3e-0928.7181 *H*S&S&H%R&R

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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