Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005198 | molecular_function | structural molecule activity |
A | 0019028 | cellular_component | viral capsid |
A | 0019031 | cellular_component | viral envelope |
A | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
A | 0039621 | cellular_component | T=13 icosahedral viral capsid |
A | 0039626 | cellular_component | viral intermediate capsid |
A | 0044423 | cellular_component | virion component |
A | 0044650 | biological_process | adhesion of symbiont to host cell |
A | 0046789 | molecular_function | host cell surface receptor binding |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 501 |
Chain | Residue |
A | HIS153 |
A | HIS153 |
A | HIS153 |
A | CL502 |
A | CL502 |
A | CL502 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL A 502 |
Chain | Residue |
A | HIS153 |
A | ZN501 |
A | ZN501 |
A | ZN501 |
A | HIS153 |
A | HIS153 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 503 |
Chain | Residue |
A | HOH874 |
A | HOH874 |
A | HOH874 |
A | HOH890 |
A | HOH890 |
A | HOH890 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 508 |
Chain | Residue |
A | ASN266 |
A | ASN266 |
A | ASP286 |
A | ASP286 |
A | HOH794 |
A | HOH794 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 601 |
Chain | Residue |
A | GLN268 |
A | GLU379 |
A | HOH652 |
A | HOH668 |
A | HOH767 |
A | HOH789 |
A | HOH845 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 602 |
Chain | Residue |
A | GLN47 |
A | ASP62 |
A | HOH681 |
A | HOH779 |
A | HOH783 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 603 |
Chain | Residue |
A | THR151 |
A | GLU340 |
A | HOH628 |
A | HOH886 |
site_id | ZNB |
Number of Residues | 1 |
Details | THE ZINC SITS ON A THREE-FOLD AXIS. THE ZINC BINDING SITE FORMED BY THREE SYMMETRICALLY-RELATED PLUS ONE WATER MOLECULE ON THE THREE-FOLD AXIS. |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS153 | |
A | ASN266 | |
A | ASP286 | |