Brand  (β version)

PDB ID: 3V3M

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
0EN N-[(1r)-2-(tert-butylamino)-2-oxo-1-(pyridin-3-yl)ethyl]-N-(4-tert-butylphenyl)furan-2-carboxamide PoSSuM
DMS Dimethyl sulfoxide PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 3V3M   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) 3CL Protease in Complex with N-[(1R)-2-(tert-butylamino)-2-oxo-1-(pyridin-3-yl)ethyl]-N-(4-tert-butylphenyl)furan-2-carboxamide inhibitor.
Release Data : 2013-01-16
Compound :
mol_id molecule chains
1 3C-like proteinase A
ec: 3.4.19.12, 3.4.22.69, 3.4.22.-
Source :
mol_id organism_scientific organism_common expression_system
1 SARS coronavirus  (taxid:227859) SARS-CoV Homo sapiens  (taxid:9606)
gene: 1a
expression_system_common: Human
Authors : Jacobs, J., Grum-Tokars, V., Zhou, Y., Turlington, M., Saldanha, S.A., Chase, P., Eggler, A., Dawson, E.S., Baez-Santos, Y.M., Tomar, S., Mielech, A.M., Baker, S.C., Lindsley, C.W., Hodder, P., Mesecar, A., Stauffer, S.R.
Keywords : Chymotrypsin like fold, viral polypeptide protease, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 1.96 Å )
Citation :

Discovery, Synthesis, And Structure-Based Optimization of a Series of N-(tert-Butyl)-2-(N-arylamido)-2-(pyridin-3-yl) Acetamides (ML188) as Potent Noncovalent Small Molecule Inhibitors of the Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) 3CL Protease.

Jacobs, J.,Grum-Tokars, V.,Zhou, Y.  et al.
(2013)  J.Med.Chem.  56 : 534 - 546

PubMed: 23231439
DOI: 10.1021/jm301580n

Reaction

Chain : A
UniProt : P0C6U8 (R1A_SARS)
Reaction: EC: Evidence:
Physiological Direction:
[3C-like proteinase nsp5]
TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position. 		3.4.22.69 PubMed:12917450, PubMed:14561748
-
[Papain-like protease nsp3]
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 PubMed:12917450, PubMed:17692280
-
[RNA-capping enzyme subunit nsp9]
a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'- end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate 		2.7.7.50 UniProtKB:P0DTC1
right-to-left
Cofactor: Evidence: Note:
Zn(2+) ECO:0000269 | PubMed:16306590
-