Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 1 | 0005198 | molecular_function | structural molecule activity |
| 2 | 0005198 | molecular_function | structural molecule activity |
| 3 | 0005198 | molecular_function | structural molecule activity |
| 4 | 0005198 | molecular_function | structural molecule activity |
| 4 | 0019028 | cellular_component | viral capsid |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ZN 1 6000 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE DAO 1 7009 |
| Chain | Residue |
| 1 | ILE98 |
| 1 | ASN99 |
| 1 | LEU100 |
| 1 | ASN212 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MYR 4 4000 |
| site_id | MYR |
| Number of Residues | 3 |
| Details | MYRISTYLATION IS OBSERVED AT N-TERMINUS OF VP4, WHICH LIES VERY CLOSE TO THE ICOSAHEDRAL FIVE-FOLD AXIS. TYR 1 6 IS HYDROGEN BONDED TO THE N-TERMINUS OF VP4 ALSO, FORMING A LINK BETWEEN THE AMPHIPATHIC HELIX AT THE TERMINUS OF VP1 AND THE 10-STRANDED BETA BARREL OBSERVED AT THE N-TERMINUS OF VP4 (TWO STRANDS, FIVE SYMMETRY RELATED COPIES). |
| Chain | Residue |
| 4 | MYR4000 |
| 4 | GLY1 |
| 1 | TYR6 |
| site_id | POC |
| Number of Residues | 4 |
| Details | A MOIETY MODELLED AS A 12-CARBON FATTY ACID IS OBSERVED IN FULL OCCUPANCY IN THE HYDROPHOBIC POCKET WHERE ANTI-VIRAL COMPOUNDS BIND. THE HEAD GROUP OXYGENS CONTACT N1212 AND L1100. |
| Chain | Residue |
| 1 | ASN212 |
| 1 | LEU100 |
| 1 | MET214 |
| 1 | DAO7009 |
| site_id | RNA |
| Number of Residues | 2 |
| Details | RNA OBSERVED INTERACTING WITH THESE RESIDUES ON INTERIOR SURFACE OF VIRAL PROTEIN CAPSID. NON-CONSERVATIVE MUTATION OF TRP 2 38 GIVES NON-VIABLE VIRUS. |
| site_id | ZN |
| Number of Residues | 3 |
| Details | PUTATIVE ZINC BINDING SITE ON ICOSAHEDRAL FIVE-FOLD AXIS. ION LIGANDED BY FIVE SYMMETRY RELATED HISTIDINES (HIS 1 134). EXTERIOR OF SITE SURROUNDED BY A WIDER CIRCLE OF FIVE HISTIDINES (HIS 1 228). |
| Chain | Residue |
| 1 | HIS134 |
| 1 | HIS228 |
| 1 | ZN6000 |
Functional Information from SwissProt/UniProt
