6I7P
Crystal structure of the full-length Zika virus NS5 protein (Human isolate Z1106033)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
| A | 0004482 | molecular_function | mRNA 5'-cap (guanine-N7-)-methyltransferase activity |
| A | 0004483 | molecular_function | mRNA (nucleoside-2'-O-)-methyltransferase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0032259 | biological_process | methylation |
| A | 0039694 | biological_process | viral RNA genome replication |
| B | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
| B | 0004482 | molecular_function | mRNA 5'-cap (guanine-N7-)-methyltransferase activity |
| B | 0004483 | molecular_function | mRNA (nucleoside-2'-O-)-methyltransferase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0039694 | biological_process | viral RNA genome replication |
| C | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
| C | 0004482 | molecular_function | mRNA 5'-cap (guanine-N7-)-methyltransferase activity |
| C | 0004483 | molecular_function | mRNA (nucleoside-2'-O-)-methyltransferase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0032259 | biological_process | methylation |
| C | 0039694 | biological_process | viral RNA genome replication |
| D | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
| D | 0004482 | molecular_function | mRNA 5'-cap (guanine-N7-)-methyltransferase activity |
| D | 0004483 | molecular_function | mRNA (nucleoside-2'-O-)-methyltransferase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0008168 | molecular_function | methyltransferase activity |
| D | 0032259 | biological_process | methylation |
| D | 0039694 | biological_process | viral RNA genome replication |
| E | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
| E | 0004482 | molecular_function | mRNA 5'-cap (guanine-N7-)-methyltransferase activity |
| E | 0004483 | molecular_function | mRNA (nucleoside-2'-O-)-methyltransferase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0008168 | molecular_function | methyltransferase activity |
| E | 0032259 | biological_process | methylation |
| E | 0039694 | biological_process | viral RNA genome replication |
| F | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
| F | 0004482 | molecular_function | mRNA 5'-cap (guanine-N7-)-methyltransferase activity |
| F | 0004483 | molecular_function | mRNA (nucleoside-2'-O-)-methyltransferase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0008168 | molecular_function | methyltransferase activity |
| F | 0032259 | biological_process | methylation |
| F | 0039694 | biological_process | viral RNA genome replication |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue SAH A 1001 |
| Chain | Residue |
| A | SER56 |
| A | HIS110 |
| A | GLU111 |
| A | VAL130 |
| A | ASP131 |
| A | VAL132 |
| A | ASP146 |
| A | ASP79 |
| A | GLY81 |
| A | CYS82 |
| A | GLY85 |
| A | GLY86 |
| A | TRP87 |
| A | THR104 |
| A | LYS105 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 A 1002 |
| Chain | Residue |
| A | LYS462 |
| A | SER712 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 A 1003 |
| Chain | Residue |
| A | ARG57 |
| A | ARG213 |
| B | LYS45 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue ZN A 1004 |
| Chain | Residue |
| A | HIS714 |
| A | CYS730 |
| A | CYS849 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 1005 |
| Chain | Residue |
| A | GLU439 |
| A | HIS443 |
| A | CYS448 |
| A | CYS451 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue SAH B 1001 |
| Chain | Residue |
| B | SER56 |
| B | GLY58 |
| B | GLY81 |
| B | CYS82 |
| B | GLY86 |
| B | TRP87 |
| B | THR104 |
| B | LYS105 |
| B | HIS110 |
| B | GLU111 |
| B | VAL130 |
| B | ASP131 |
| B | VAL132 |
| B | ASP146 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 B 1002 |
| Chain | Residue |
| A | LYS45 |
| B | ARG41 |
| B | ARG57 |
| B | ARG213 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 B 1003 |
| Chain | Residue |
| B | HIS855 |
| B | ARG856 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 1004 |
| Chain | Residue |
| B | HIS714 |
| B | ASN716 |
| B | CYS730 |
| B | CYS849 |
| site_id | AD1 |
| Number of Residues | 12 |
| Details | binding site for residue SAH C 1001 |
| Chain | Residue |
| C | SER56 |
| C | GLY58 |
| C | GLY81 |
| C | CYS82 |
| C | GLY83 |
| C | TRP87 |
| C | THR104 |
| C | LYS105 |
| C | HIS110 |
| C | VAL130 |
| C | ASP131 |
| C | ASP146 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 C 1002 |
| Chain | Residue |
| C | LYS76 |
| C | LYS101 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 1003 |
| Chain | Residue |
| C | HIS714 |
| C | ASN716 |
| C | CYS730 |
| C | CYS849 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 1004 |
| Chain | Residue |
| C | GLU439 |
| C | HIS443 |
| C | CYS448 |
| C | CYS451 |
| site_id | AD5 |
| Number of Residues | 11 |
| Details | binding site for residue SAH D 1001 |
| Chain | Residue |
| D | SER56 |
| D | GLY58 |
| D | GLY81 |
| D | CYS82 |
| D | GLY86 |
| D | TRP87 |
| D | THR104 |
| D | LYS105 |
| D | VAL130 |
| D | ASP131 |
| D | ASP146 |
| site_id | AD6 |
| Number of Residues | 1 |
| Details | binding site for residue PO4 D 1002 |
| Chain | Residue |
| D | LYS101 |
| site_id | AD7 |
| Number of Residues | 1 |
| Details | binding site for residue PO4 D 1003 |
| Chain | Residue |
| D | ARG125 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 D 1004 |
| Chain | Residue |
| D | LYS470 |
| D | ARG473 |
| D | LYS691 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 D 1005 |
| Chain | Residue |
| D | SER712 |
| D | ARG731 |
| D | ARG739 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue ZN D 1006 |
| Chain | Residue |
| D | HIS714 |
| D | CYS730 |
| D | CYS849 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN D 1007 |
| Chain | Residue |
| D | CYS451 |
| D | GLU439 |
| D | HIS443 |
| D | CYS448 |
| D | SER450 |
| site_id | AE3 |
| Number of Residues | 11 |
| Details | binding site for residue SAH E 1001 |
| Chain | Residue |
| E | SER56 |
| E | GLY81 |
| E | CYS82 |
| E | GLY85 |
| E | GLY86 |
| E | TRP87 |
| E | THR104 |
| E | LYS105 |
| E | HIS110 |
| E | VAL132 |
| E | ASP146 |
| site_id | AE4 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 E 1002 |
| Chain | Residue |
| E | ARG57 |
| E | ARG213 |
| F | LYS45 |
| site_id | AE5 |
| Number of Residues | 1 |
| Details | binding site for residue PO4 E 1003 |
| Chain | Residue |
| E | HIS855 |
| site_id | AE6 |
| Number of Residues | 3 |
| Details | binding site for residue ZN E 1004 |
| Chain | Residue |
| E | HIS714 |
| E | CYS730 |
| E | CYS849 |
| site_id | AE7 |
| Number of Residues | 6 |
| Details | binding site for residue ZN E 1005 |
| Chain | Residue |
| E | GLU439 |
| E | HIS443 |
| E | CYS448 |
| E | GLN449 |
| E | SER450 |
| E | CYS451 |
| site_id | AE8 |
| Number of Residues | 12 |
| Details | binding site for residue SAH F 1001 |
| Chain | Residue |
| F | SER56 |
| F | GLY81 |
| F | CYS82 |
| F | GLY86 |
| F | TRP87 |
| F | THR104 |
| F | LYS105 |
| F | HIS110 |
| F | VAL130 |
| F | PHE133 |
| F | ASP146 |
| F | ILE147 |
| site_id | AE9 |
| Number of Residues | 1 |
| Details | binding site for residue PO4 F 1002 |
| Chain | Residue |
| F | SER712 |
| site_id | AF1 |
| Number of Residues | 1 |
| Details | binding site for residue PO4 F 1003 |
| Chain | Residue |
| F | LYS691 |
| site_id | AF2 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 F 1004 |
| Chain | Residue |
| F | LYS76 |
| F | GLU99 |
| F | LYS101 |
| site_id | AF3 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 F 1005 |
| Chain | Residue |
| F | LYS101 |
| F | ARG125 |
| site_id | AF4 |
| Number of Residues | 5 |
| Details | binding site for residue ZN F 1006 |
| Chain | Residue |
| F | HIS714 |
| F | ASN716 |
| F | CYS730 |
| F | LEU841 |
| F | CYS849 |
| site_id | AF5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN F 1007 |
| Chain | Residue |
| F | GLU439 |
| F | HIS443 |
| F | CYS448 |
| F | CYS451 |
| site_id | AF6 |
| Number of Residues | 13 |
| Details | binding site for Di-peptide GLU B 417 and TRP B 479 |
| Chain | Residue |
| B | GLY411 |
| B | ALA412 |
| B | ILE413 |
| B | PHE414 |
| B | GLU415 |
| B | GLU416 |
| B | LYS418 |
| B | GLU419 |
| B | MET478 |
| B | LEU480 |
| B | GLY481 |
| B | ALA482 |
| B | ARG483 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | ACT_SITE: For 2'-O-MTase activity => ECO:0000250|UniProtKB:Q6YMS4 |
| Chain | Residue | Details |
| A | LYS61 | |
| C | ASP146 | |
| C | LYS182 | |
| C | GLU218 | |
| D | LYS61 | |
| D | ASP146 | |
| D | LYS182 | |
| D | GLU218 | |
| E | LYS61 | |
| E | ASP146 | |
| E | LYS182 | |
| A | ASP146 | |
| E | GLU218 | |
| F | LYS61 | |
| F | ASP146 | |
| F | LYS182 | |
| F | GLU218 | |
| A | LYS182 | |
| A | GLU218 | |
| B | LYS61 | |
| B | ASP146 | |
| B | LYS182 | |
| B | GLU218 | |
| C | LYS61 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27866982 |
| Chain | Residue | Details |
| A | LYS13 | |
| D | LYS13 | |
| D | GLU149 | |
| D | ARG213 | |
| E | LYS13 | |
| E | GLU149 | |
| E | ARG213 | |
| F | LYS13 | |
| F | GLU149 | |
| F | ARG213 | |
| A | GLU149 | |
| A | ARG213 | |
| B | LYS13 | |
| B | GLU149 | |
| B | ARG213 | |
| C | LYS13 | |
| C | GLU149 | |
| C | ARG213 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:27866982 |
| Chain | Residue | Details |
| A | SER56 | |
| E | THR104 | |
| F | SER56 | |
| F | THR104 | |
| A | THR104 | |
| B | SER56 | |
| B | THR104 | |
| C | SER56 | |
| C | THR104 | |
| D | SER56 | |
| D | THR104 | |
| E | SER56 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 30 |
| 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 | |
| D | GLY86 | |
| D | TRP87 | |
| D | LYS105 | |
| D | ASP131 | |
| A | TRP87 | |
| D | VAL132 | |
| E | GLY86 | |
| E | TRP87 | |
| E | LYS105 | |
| E | ASP131 | |
| E | VAL132 | |
| F | GLY86 | |
| F | TRP87 | |
| F | LYS105 | |
| F | ASP131 | |
| A | LYS105 | |
| F | VAL132 | |
| A | ASP131 | |
| A | VAL132 | |
| B | GLY86 | |
| B | TRP87 | |
| B | LYS105 | |
| B | ASP131 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27633330, ECO:0000269|PubMed:27866982, ECO:0000269|PubMed:28031359 |
| Chain | Residue | Details |
| A | HIS110 | |
| D | HIS110 | |
| D | GLU111 | |
| D | ASP146 | |
| E | HIS110 | |
| E | GLU111 | |
| E | ASP146 | |
| F | HIS110 | |
| F | GLU111 | |
| F | ASP146 | |
| A | GLU111 | |
| A | ASP146 | |
| B | HIS110 | |
| B | GLU111 | |
| B | ASP146 | |
| C | HIS110 | |
| C | GLU111 | |
| C | ASP146 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00924 |
| Chain | Residue | Details |
| A | ILE147 | |
| E | TYR220 | |
| F | ILE147 | |
| F | TYR220 | |
| A | TYR220 | |
| B | ILE147 | |
| B | TYR220 | |
| C | ILE147 | |
| C | TYR220 | |
| D | ILE147 | |
| D | TYR220 | |
| E | ILE147 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 36 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q32ZE1 |
| Chain | Residue | Details |
| A | GLU439 | |
| B | CYS451 | |
| B | HIS714 | |
| B | CYS730 | |
| C | GLU439 | |
| C | HIS443 | |
| C | CYS448 | |
| C | CYS451 | |
| C | HIS714 | |
| C | CYS730 | |
| D | GLU439 | |
| A | HIS443 | |
| D | HIS443 | |
| D | CYS448 | |
| D | CYS451 | |
| D | HIS714 | |
| D | CYS730 | |
| E | GLU439 | |
| E | HIS443 | |
| E | CYS448 | |
| E | CYS451 | |
| E | HIS714 | |
| A | CYS448 | |
| E | CYS730 | |
| F | GLU439 | |
| F | HIS443 | |
| F | CYS448 | |
| F | CYS451 | |
| F | HIS714 | |
| F | CYS730 | |
| A | CYS451 | |
| A | HIS714 | |
| A | CYS730 | |
| B | GLU439 | |
| B | HIS443 | |
| B | CYS448 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P14335 |
| Chain | Residue | Details |
| A | CYS849 | |
| B | CYS849 | |
| C | CYS849 | |
| D | CYS849 | |
| E | CYS849 | |
| F | CYS849 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 42 |
| 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 | |
| D | LYS13 | |
| D | ASN17 | |
| D | PHE24 | |
| D | LYS28 | |
| D | SER150 | |
| D | ARG213 | |
| D | SER215 | |
| E | LYS13 | |
| A | PHE24 | |
| E | ASN17 | |
| E | PHE24 | |
| E | LYS28 | |
| E | SER150 | |
| E | ARG213 | |
| E | SER215 | |
| F | LYS13 | |
| F | ASN17 | |
| F | PHE24 | |
| F | LYS28 | |
| A | LYS28 | |
| F | SER150 | |
| F | ARG213 | |
| F | SER215 | |
| A | SER150 | |
| A | ARG213 | |
| A | SER215 | |
| B | LYS13 | |
| B | ASN17 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 12 |
| Details | SITE: mRNA cap binding; via carbonyl oxygen => ECO:0000255|PROSITE-ProRule:PRU00924 |
| Chain | Residue | Details |
| A | LEU16 | |
| E | MET19 | |
| F | LEU16 | |
| F | MET19 | |
| A | MET19 | |
| B | LEU16 | |
| B | MET19 | |
| C | LEU16 | |
| C | MET19 | |
| D | LEU16 | |
| D | MET19 | |
| E | LEU16 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 18 |
| Details | SITE: Essential for 2'-O-methyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU00924 |
| Chain | Residue | Details |
| A | LYS61 | |
| D | LYS61 | |
| D | LYS182 | |
| D | GLU218 | |
| E | LYS61 | |
| E | LYS182 | |
| E | GLU218 | |
| F | LYS61 | |
| F | LYS182 | |
| F | GLU218 | |
| A | LYS182 | |
| A | GLU218 | |
| B | LYS61 | |
| B | LYS182 | |
| B | GLU218 | |
| C | LYS61 | |
| C | LYS182 | |
| C | GLU218 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 6 |
| 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 | |
| D | ASP146 | |
| E | ASP146 | |
| F | ASP146 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P03314 |
| Chain | Residue | Details |
| A | SER56 | |
| B | SER56 | |
| C | SER56 | |
| D | SER56 | |
| E | SER56 | |
| F | SER56 |
