3EVD
Crystal structure of GTP complex of yellow fever virus methyltransferase and S-adenosyl-L-homocysteine
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE GTP A 901 |
| Chain | Residue |
| A | LYS13 |
| A | ARG213 |
| A | SER215 |
| A | HOH516 |
| A | HOH650 |
| A | HOH677 |
| A | LEU16 |
| A | ASN17 |
| A | LEU19 |
| A | PHE24 |
| A | LYS28 |
| A | SER150 |
| A | SER151 |
| A | SER152 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GTP A 902 |
| Chain | Residue |
| A | ARG37 |
| A | ARG41 |
| A | SER56 |
| A | ARG57 |
| A | ARG84 |
| A | HOH672 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE SAH A 903 |
| Chain | Residue |
| A | SER56 |
| A | GLY58 |
| A | GLY81 |
| A | CYS82 |
| A | GLY83 |
| A | GLY86 |
| A | TRP87 |
| A | THR104 |
| A | LEU105 |
| A | HIS110 |
| A | THR130 |
| A | ASP131 |
| A | ILE132 |
| A | HIS133 |
| A | ASP146 |
| A | ILE147 |
| A | HOH520 |
| A | HOH546 |
| A | HOH574 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"For 2'-O-MTase activity","evidences":[{"source":"UniProtKB","id":"Q6YMS4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00924","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Site: {"description":"mRNA cap binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00924","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19101564","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"mRNA cap binding; via carbonyl oxygen","evidences":[{"source":"PROSITE-ProRule","id":"PRU00924","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19101564","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"mRNA cap binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00924","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Site: {"description":"Essential for 2'-O-methyltransferase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU00924","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Site: {"description":"Essential for 2'-O-methyltransferase and N-7 methyltransferase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU00924","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18757072","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18757072","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
