1AYM
HUMAN RHINOVIRUS 16 COAT PROTEIN AT HIGH RESOLUTION
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ZN 1 6000 |
| Chain | Residue |
| 1 | HIS134 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MYR 4 4000 |
| Chain | Residue |
| 4 | GLY1 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DAO 1 7009 |
| Chain | Residue |
| 1 | ILE98 |
| 1 | ASN99 |
| 1 | LEU100 |
| 1 | SER120 |
| 1 | ILE122 |
| 1 | ASN212 |
| 1 | MET214 |
| 1 | HOH5377 |
| 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 | PO2 |
| Number of Residues | 3 |
| Details | STRAND H IN VP1 IS OBSERVED IN TWO CONFORMATIONS, DEPENDING ON WHETHER THE FATTY ACID IS PRESENT OR NOT. CONFORMATION A (1 210 A -1 218 A) REPRESENTS THE OPEN FORM OF THE POCKET WITH THE FATTY ACID PRESENT AND RESEMBLES THE STRUCTURE ORIGINALLY OBSERVED IN HRV16 (2RHN), HRV1A, CVB3, POLIO STRAINS. CONFORMATION B (1 101 B - 1 218 B) REPRESENT THE CLOSED FORM OF THE POCKET WHICH RESEMBLES THE NATIVE STRUCTURE OF HRV14 MORE CLOSELY. A WATER MOLECULE (HOH 5 377) IS MODELLED IN THE POSITION OF THE FATTY ACID HEAD GROUP IN THE CLOSED CONFORMATION. THIS DUAL OCCUPANCY IS NOT OBSERVED USING THE DATA SET WHICH THE MODEL 2RHN WAS BASED ON. |
| Chain | Residue |
| 1 | DAO7009 |
| 1 | MET112 |
| 1 | HOH5377 |
| site_id | POC |
| Number of Residues | 4 |
| Details | A MOIETY MODELLED AS A 12-CARBON FATTY ACID IS OBSERVED IN PARTIAL 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. |
| Chain | Residue |
| 2 | TRP38 |
| 3 | PHE35 |
| 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
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | LIPID: N-myristoyl glycine; by host => ECO:0000250|UniProtKB:P03300 |
| Chain | Residue | Details |
| 4 | ALA2 |
