Protein Data Bank in Europe

[a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleosidein mRNA + S-adenosyl-L-homocysteine., a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleosidein mRNA + S-adenosyl-L-homocysteine., a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleosidein mRNA + S-adenosyl-L-homocysteine., a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleosidein mRNA + S-adenosyl-L-homocysteine., a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleosidein mRNA + S-adenosyl-L-homocysteine., a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleosidein mRNA + S-adenosyl-L-homocysteine., a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleosidein mRNA + S-adenosyl-L-homocysteine., a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleosidein mRNA + S-adenosyl-L-homocysteine.]

[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(+)., 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(+)., 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(+)., 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(+)., 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(+)., 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(+)., 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(+)., 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(+).]

[RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate., RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate., RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate., RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate., RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate., RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate., RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate., RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate.]

[a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end(5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate., a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end(5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate., a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end(5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate., a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end(5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate., a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end(5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate., a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end(5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate., a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end(5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate., a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end(5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate.]

[Thiol-dependent hydrolysis of ester, thioester, amide, peptide andisopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residueprotein attached to proteins as an intracellular targeting signal)., Thiol-dependent hydrolysis of ester, thioester, amide, peptide andisopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residueprotein attached to proteins as an intracellular targeting signal)., Thiol-dependent hydrolysis of ester, thioester, amide, peptide andisopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residueprotein attached to proteins as an intracellular targeting signal)., Thiol-dependent hydrolysis of ester, thioester, amide, peptide andisopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residueprotein attached to proteins as an intracellular targeting signal)., Thiol-dependent hydrolysis of ester, thioester, amide, peptide andisopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residueprotein attached to proteins as an intracellular targeting signal)., Thiol-dependent hydrolysis of ester, thioester, amide, peptide andisopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residueprotein attached to proteins as an intracellular targeting signal)., Thiol-dependent hydrolysis of ester, thioester, amide, peptide andisopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residueprotein attached to proteins as an intracellular targeting signal)., Thiol-dependent hydrolysis of ester, thioester, amide, peptide andisopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residueprotein attached to proteins as an intracellular targeting signal).]

[TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides corresponding tothe two self-cleavage sites of the SARS 3C-like proteinase are the twomost reactive peptide substrates. The enzyme exhibits a strong preferencefor substrates containing Gln at P1 position and Leu at P2 position., TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides corresponding tothe two self-cleavage sites of the SARS 3C-like proteinase are the twomost reactive peptide substrates. The enzyme exhibits a strong preferencefor substrates containing Gln at P1 position and Leu at P2 position., TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides corresponding tothe two self-cleavage sites of the SARS 3C-like proteinase are the twomost reactive peptide substrates. The enzyme exhibits a strong preferencefor substrates containing Gln at P1 position and Leu at P2 position., TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides corresponding tothe two self-cleavage sites of the SARS 3C-like proteinase are the twomost reactive peptide substrates. The enzyme exhibits a strong preferencefor substrates containing Gln at P1 position and Leu at P2 position., TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides corresponding tothe two self-cleavage sites of the SARS 3C-like proteinase are the twomost reactive peptide substrates. The enzyme exhibits a strong preferencefor substrates containing Gln at P1 position and Leu at P2 position., TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides corresponding tothe two self-cleavage sites of the SARS 3C-like proteinase are the twomost reactive peptide substrates. The enzyme exhibits a strong preferencefor substrates containing Gln at P1 position and Leu at P2 position., TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides corresponding tothe two self-cleavage sites of the SARS 3C-like proteinase are the twomost reactive peptide substrates. The enzyme exhibits a strong preferencefor substrates containing Gln at P1 position and Leu at P2 position., TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides corresponding tothe two self-cleavage sites of the SARS 3C-like proteinase are the twomost reactive peptide substrates. The enzyme exhibits a strong preferencefor substrates containing Gln at P1 position and Leu at P2 position.]

[ATP + H2O = ADP + phosphate + H(+)., ATP + H2O = ADP + phosphate + H(+)., ATP + H2O = ADP + phosphate + H(+)., ATP + H2O = ADP + phosphate + H(+)., ATP + H2O = ADP + phosphate + H(+)., ATP + H2O = ADP + phosphate + H(+)., ATP + H2O = ADP + phosphate + H(+)., ATP + H2O = ADP + phosphate + H(+).]