Brand  (β version)

PDB ID: 4ZRO

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Ligands
Code Name Style Show Link
DMS Dimethyl sulfoxide PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
BOC Tert-butyl hydrogen carbonate
CEV Ethyl (4r)-4-amino-5-[(3s)-2-oxopyrrolidin-3-yl]pentanoate

Structure summary

Code : 4ZRO   PDBj   RCSB PDB   PDBe
Header : Hydrolase/Hydrolase Inhibitor
Title : 2.1 A X-Ray Structure of FIPV-3CLpro bound to covalent inhibitor
Release Data : 2015-10-14
Compound :
mol_id molecule chains synonym
1 3C-like proteinase A,B,C,D 3CL-PRO, 3CLp, M-PRO, nsp5
ec: 3.4.22.-
mol_id molecule chains
2 Bounded inhibitor of N-(tert-butoxycarbonyl)-L-seryl-L-valyl-N-{(2S)-5-ethoxy-5-oxo-1-[(3S)-2-oxopyrrolidin-3-yl]pentan-2-yl}-L-leucinamide E,F,G,H
Source :
mol_id organism_scientific organism_common expression_system
1 Feline coronavirus (strain FIPV WSU-79/1146)  (taxid:33734) FCoV Escherichia coli  (taxid:562)
strain: FIPV WSU-79/1146
gene: rep, 1a-1b
mol_id organism_scientific
2 Synthetic construct  (taxid:32630)
synthetic: yes
Authors : St John, S.E., Mesecar, A.D.
Keywords : Coronavirus, main protease, 3CLpro, Mpro, FIPV, FCoV, inhibitor complex, feline infectious peritonitis, Hydrolase-Hydrolase Inhibitor complex
Exp. method : X-RAY DIFFRACTION ( 2.0566 Å )
Citation :

X-ray structure and inhibition of the feline infectious peritonitis virus 3C-like protease: Structural implications for drug design.

St John, S.E.,Therkelsen, M.D.,Nyalapatla, P.R.  et al.
(2015)  Bioorg.Med.Chem.Lett.  25 : 5072 - 5077

PubMed: 26592814
DOI: 10.1016/j.bmcl.2015.10.023

Reaction

Chain : A, B, C, D
UniProt : Q98VG9 (R1AB_FIPV)
Reaction: EC: Evidence:
Physiological Direction:
[Non-structural protein 3]
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- residue protein attached to proteins as an intracellular targeting signal). 		3.4.19.12 -
-
[RNA-directed RNA polymerase nsp12]
RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate 		2.7.7.48 -
-
[Helicase]
ATP + H2O = ADP + phosphate + H(+) 		3.6.4.12 -
-
[Helicase]
ATP + H2O = ADP + phosphate + H(+) 		3.6.4.13 -
-
[RNA-directed RNA polymerase nsp12]
a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'- end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate 		2.7.7.50 UniProtKB:P0DTD1
left-to-right
[Putative 2'-O-methyl transferase]
a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'- triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + S- adenosyl-L-homocysteine + H(+) 		2.1.1.57 UniProtKB:P0C6X7
-
[Uridylate-specific endoribonuclease]
uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl- 2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside- RNA 		- UniProtKB:P0C6X7
-
Cofactor: Evidence: Note:
Mn(2+) ECO:0000250 | UniProtKB:P0C6X7
Likely affects Nsp15 binding to RNA.