3EVB
Crystal structure of yellow fever virus methyltransferase complexed with S-adenosyl-L-homocysteine
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE SAH A 901 |
Chain | Residue |
A | SER56 |
A | HIS110 |
A | THR130 |
A | ASP131 |
A | ILE132 |
A | HIS133 |
A | ASP146 |
A | ILE147 |
A | HOH520 |
A | HOH546 |
A | HOH565 |
A | GLY58 |
A | HOH574 |
A | HOH604 |
A | HOH704 |
A | GLY81 |
A | CYS82 |
A | GLY83 |
A | GLY86 |
A | TRP87 |
A | THR104 |
A | LEU105 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: For 2'-O-MTase activity => ECO:0000250|UniProtKB:Q6YMS4 |
Chain | Residue | Details |
A | LYS61 | |
A | ASP146 | |
A | LYS182 | |
A | GLU218 |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00924 |
Chain | Residue | Details |
A | SER56 | |
A | ASP131 | |
A | ILE132 | |
A | ILE147 | |
A | TYR220 | |
A | GLY86 | |
A | TRP87 | |
A | THR104 | |
A | LEU105 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | SITE: mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:19101564 |
Chain | Residue | Details |
A | ARG213 | |
A | SER215 | |
A | LYS13 | |
A | ASN17 | |
A | LYS28 | |
A | SER150 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: mRNA cap binding; via carbonyl oxygen => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:19101564 |
Chain | Residue | Details |
A | LEU16 | |
A | LEU19 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924 |
Chain | Residue | Details |
A | PHE24 |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | SITE: Essential for 2'-O-methyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU00924 |
Chain | Residue | Details |
A | LYS182 | |
A | GLU218 | |
A | LYS61 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | SITE: Essential for 2'-O-methyltransferase and N-7 methyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:18757072 |
Chain | Residue | Details |
A | ASP146 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:18757072 |
Chain | Residue | Details |
A | SER56 |