5GOZ
Crystal structure of ZIKV NS5 Methyltransferase in complex with GTP and SAH
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004482 | molecular_function | mRNA 5'-cap (guanine-N7-)-methyltransferase activity |
A | 0004483 | molecular_function | mRNA (nucleoside-2'-O-)-methyltransferase activity |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0032259 | biological_process | methylation |
B | 0004482 | molecular_function | mRNA 5'-cap (guanine-N7-)-methyltransferase activity |
B | 0004483 | molecular_function | mRNA (nucleoside-2'-O-)-methyltransferase activity |
B | 0008168 | molecular_function | methyltransferase activity |
B | 0032259 | biological_process | methylation |
C | 0004482 | molecular_function | mRNA 5'-cap (guanine-N7-)-methyltransferase activity |
C | 0004483 | molecular_function | mRNA (nucleoside-2'-O-)-methyltransferase activity |
C | 0008168 | molecular_function | methyltransferase activity |
C | 0032259 | biological_process | methylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue GTP A 301 |
Chain | Residue |
A | LYS13 |
A | SER215 |
A | HOH440 |
A | HOH451 |
A | LEU16 |
A | ASN17 |
A | MET19 |
A | PHE24 |
A | SER150 |
A | SER151 |
A | SER152 |
A | ARG213 |
site_id | AC2 |
Number of Residues | 17 |
Details | binding site for residue SAH A 302 |
Chain | Residue |
A | SER56 |
A | GLY58 |
A | GLY81 |
A | CYS82 |
A | GLY83 |
A | GLY86 |
A | TRP87 |
A | THR104 |
A | LYS105 |
A | HIS110 |
A | GLU111 |
A | VAL130 |
A | ASP131 |
A | VAL132 |
A | PHE133 |
A | ASP146 |
A | HOH403 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue PO4 A 303 |
Chain | Residue |
A | ARG37 |
A | ARG41 |
A | SER56 |
A | ARG57 |
A | ARG84 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue PO4 A 304 |
Chain | Residue |
A | LYS29 |
A | ARG41 |
A | ARG57 |
A | ARG213 |
site_id | AC5 |
Number of Residues | 13 |
Details | binding site for residue GTP B 301 |
Chain | Residue |
B | LYS13 |
B | LEU16 |
B | ASN17 |
B | MET19 |
B | PHE24 |
B | LYS28 |
B | SER150 |
B | SER151 |
B | SER152 |
B | ARG213 |
B | SER215 |
B | HOH415 |
B | HOH425 |
site_id | AC6 |
Number of Residues | 16 |
Details | binding site for residue SAH B 302 |
Chain | Residue |
B | SER56 |
B | GLY58 |
B | GLY81 |
B | CYS82 |
B | GLY83 |
B | GLY86 |
B | TRP87 |
B | LYS105 |
B | HIS110 |
B | GLU111 |
B | VAL130 |
B | ASP131 |
B | VAL132 |
B | PHE133 |
B | ASP146 |
B | HOH416 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue SIN B 303 |
Chain | Residue |
A | ARG197 |
B | GLN72 |
B | TYR74 |
B | LYS96 |
B | SIN304 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue SIN B 304 |
Chain | Residue |
A | ARG201 |
B | LYS96 |
B | SIN303 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue PO4 B 306 |
Chain | Residue |
B | ARG37 |
B | ARG41 |
B | ARG57 |
B | ARG84 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue GTP C 301 |
Chain | Residue |
C | LYS13 |
C | LEU16 |
C | ASN17 |
C | MET19 |
C | PHE24 |
C | LYS28 |
C | SER151 |
C | SER152 |
C | SER215 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue GTP C 302 |
Chain | Residue |
C | GLU149 |
C | SER151 |
C | SER152 |
C | SER153 |
C | GLU155 |
C | VAL156 |
C | ARG160 |
C | ARG249 |
site_id | AD3 |
Number of Residues | 16 |
Details | binding site for residue SAH C 303 |
Chain | Residue |
C | CYS82 |
C | GLY86 |
C | TRP87 |
C | THR104 |
C | LYS105 |
C | HIS110 |
C | VAL130 |
C | ASP131 |
C | VAL132 |
C | PHE133 |
C | ASP146 |
C | HOH408 |
C | HOH409 |
C | SER56 |
C | GLY58 |
C | GLY81 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue SIN C 304 |
Chain | Residue |
C | GLN72 |
C | TYR74 |
C | LYS96 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue POP C 305 |
Chain | Residue |
C | ARG41 |
C | SER56 |
C | ARG57 |
C | ARG84 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue PO4 C 306 |
Chain | Residue |
C | LYS29 |
C | ARG41 |
C | ARG57 |
C | ARG213 |
site_id | AD7 |
Number of Residues | 8 |
Details | binding site for Di-peptide PO4 B 305 and LYS B 29 |
Chain | Residue |
B | TYR27 |
B | LYS28 |
B | SER30 |
B | GLY31 |
B | ILE32 |
B | GLU34 |
B | ARG213 |
B | VAL251 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | ACT_SITE: For 2'-O-MTase activity => ECO:0000250|UniProtKB:Q6YMS4 |
Chain | Residue | Details |
A | LYS61 | |
C | ASP146 | |
C | LYS182 | |
C | GLU218 | |
A | ASP146 | |
A | LYS182 | |
A | GLU218 | |
B | LYS61 | |
B | ASP146 | |
B | LYS182 | |
B | GLU218 | |
C | LYS61 |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27866982 |
Chain | Residue | Details |
A | LYS13 | |
A | GLU149 | |
A | ARG213 | |
B | LYS13 | |
B | GLU149 | |
B | ARG213 | |
C | LYS13 | |
C | GLU149 | |
C | ARG213 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:27866982 |
Chain | Residue | Details |
A | SER56 | |
A | THR104 | |
B | SER56 | |
B | THR104 | |
C | SER56 | |
C | THR104 |
site_id | SWS_FT_FI4 |
Number of Residues | 15 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:27633330, ECO:0000269|PubMed:27866982, ECO:0000269|PubMed:28031359 |
Chain | Residue | Details |
A | GLY86 | |
B | VAL132 | |
C | GLY86 | |
C | TRP87 | |
C | LYS105 | |
C | ASP131 | |
C | VAL132 | |
A | TRP87 | |
A | LYS105 | |
A | ASP131 | |
A | VAL132 | |
B | GLY86 | |
B | TRP87 | |
B | LYS105 | |
B | ASP131 |
site_id | SWS_FT_FI5 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27633330, ECO:0000269|PubMed:27866982, ECO:0000269|PubMed:28031359 |
Chain | Residue | Details |
A | HIS110 | |
A | GLU111 | |
A | ASP146 | |
B | HIS110 | |
B | GLU111 | |
B | ASP146 | |
C | HIS110 | |
C | GLU111 | |
C | ASP146 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00924 |
Chain | Residue | Details |
A | ILE147 | |
A | TYR220 | |
B | ILE147 | |
B | TYR220 | |
C | ILE147 | |
C | TYR220 |
site_id | SWS_FT_FI7 |
Number of Residues | 21 |
Details | SITE: mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924 |
Chain | Residue | Details |
A | LYS13 | |
B | PHE24 | |
B | LYS28 | |
B | SER150 | |
B | ARG213 | |
B | SER215 | |
C | LYS13 | |
C | ASN17 | |
C | PHE24 | |
C | LYS28 | |
C | SER150 | |
A | ASN17 | |
C | ARG213 | |
C | SER215 | |
A | PHE24 | |
A | LYS28 | |
A | SER150 | |
A | ARG213 | |
A | SER215 | |
B | LYS13 | |
B | ASN17 |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | SITE: mRNA cap binding; via carbonyl oxygen => ECO:0000255|PROSITE-ProRule:PRU00924 |
Chain | Residue | Details |
A | LEU16 | |
A | MET19 | |
B | LEU16 | |
B | MET19 | |
C | LEU16 | |
C | MET19 |
site_id | SWS_FT_FI9 |
Number of Residues | 9 |
Details | SITE: Essential for 2'-O-methyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU00924 |
Chain | Residue | Details |
A | LYS61 | |
A | LYS182 | |
A | GLU218 | |
B | LYS61 | |
B | LYS182 | |
B | GLU218 | |
C | LYS61 | |
C | LYS182 | |
C | GLU218 |
site_id | SWS_FT_FI10 |
Number of Residues | 3 |
Details | SITE: Essential for 2'-O-methyltransferase and N-7 methyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU00924 |
Chain | Residue | Details |
A | ASP146 | |
B | ASP146 | |
C | ASP146 |
site_id | SWS_FT_FI11 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P03314 |
Chain | Residue | Details |
A | SER56 | |
B | SER56 | |
C | SER56 |