2zu2: Difference between revisions

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 ==complex structure of CoV 229E 3CL protease with EPDTC==
-<StructureSection load='2zu2' size='340' side='right' caption='[[2zu2]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='2zu2' size='340' side='right'caption='[[2zu2]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2zu2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cvh22 Cvh22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZU2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZU2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2zu2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_coronavirus_229E Human coronavirus 229E]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZU2 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTZ:ZINC(II)HYDROGENSULFIDE'>DTZ</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ztx|2ztx]], [[2zty|2zty]], [[2ztz|2ztz]], [[2zu1|2zu1]], [[2zu3|2zu3]], [[2zu4|2zu4]], [[2zu5|2zu5]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTZ:ZINC(II)HYDROGENSULFIDE'>DTZ</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zu2 OCA], [http://pdbe.org/2zu2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zu2 RCSB], [http://www.ebi.ac.uk/pdbsum/2zu2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zu2 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zu2 OCA], [https://pdbe.org/2zu2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zu2 RCSB], [https://www.ebi.ac.uk/pdbsum/2zu2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zu2 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/R1A_CVH22 R1A_CVH22]] The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 (By similarity).  The main proteinase 3CL-PRO is responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity).  Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter (By similarity).  Nsp9 is a ssRNA-binding protein (By similarity).
+[https://www.uniprot.org/uniprot/R1A_CVH22 R1A_CVH22] The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 (By similarity).  The main proteinase 3CL-PRO is responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity).  Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter (By similarity).  Nsp9 is a ssRNA-binding protein (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 ==See Also==
-*[[SARS Coronavirus Main Proteinase|SARS Coronavirus Main Proteinase]]
+*[[Virus protease 3D structures|Virus protease 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Cvh22]]
+[[Category: Human coronavirus 229E]]
-[[Category: Lee, C C]]
+[[Category: Large Structures]]
-[[Category: Wang, A H.J]]
+[[Category: Lee CC]]
-[[Category: Hydrolase]]
+[[Category: Wang AH-J]]
-[[Category: Hydrolase-hydrolase inhibitor complex]]
-[[Category: Metal-binding]]
-[[Category: Protease]]
-[[Category: Protease-inhibitor complex]]
-[[Category: Thiol protease]]