2XC1
Full-length Tailspike Protein Mutant Y108W of Bacteriophage P22
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0019062 | biological_process | virion attachment to host cell |
| A | 0044409 | biological_process | symbiont entry into host |
| A | 0044423 | cellular_component | virion component |
| A | 0046718 | biological_process | symbiont entry into host cell |
| A | 0052775 | molecular_function | endo-1,3-alpha-L-rhamnosidase activity |
| A | 0098015 | cellular_component | virus tail |
| A | 0098024 | cellular_component | virus tail, fiber |
| A | 0098671 | biological_process | adhesion receptor-mediated virion attachment to host cell |
| A | 0098994 | biological_process | symbiont entry into host cell via disruption of host cell envelope |
| A | 0098995 | biological_process | symbiont entry into host cell via disruption of host cell envelope lipopolysaccharide |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0019062 | biological_process | virion attachment to host cell |
| B | 0044409 | biological_process | symbiont entry into host |
| B | 0044423 | cellular_component | virion component |
| B | 0046718 | biological_process | symbiont entry into host cell |
| B | 0052775 | molecular_function | endo-1,3-alpha-L-rhamnosidase activity |
| B | 0098015 | cellular_component | virus tail |
| B | 0098024 | cellular_component | virus tail, fiber |
| B | 0098671 | biological_process | adhesion receptor-mediated virion attachment to host cell |
| B | 0098994 | biological_process | symbiont entry into host cell via disruption of host cell envelope |
| B | 0098995 | biological_process | symbiont entry into host cell via disruption of host cell envelope lipopolysaccharide |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0019062 | biological_process | virion attachment to host cell |
| C | 0044409 | biological_process | symbiont entry into host |
| C | 0044423 | cellular_component | virion component |
| C | 0046718 | biological_process | symbiont entry into host cell |
| C | 0052775 | molecular_function | endo-1,3-alpha-L-rhamnosidase activity |
| C | 0098015 | cellular_component | virus tail |
| C | 0098024 | cellular_component | virus tail, fiber |
| C | 0098671 | biological_process | adhesion receptor-mediated virion attachment to host cell |
| C | 0098994 | biological_process | symbiont entry into host cell via disruption of host cell envelope |
| C | 0098995 | biological_process | symbiont entry into host cell via disruption of host cell envelope lipopolysaccharide |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1667 |
| Chain | Residue |
| A | SER568 |
| A | LYS569 |
| A | THR570 |
| A | LEU571 |
| C | TYR74 |
| C | ASN75 |
| C | HOH2084 |
| C | HOH2086 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1668 |
| Chain | Residue |
| A | GLU469 |
| A | GLY494 |
| A | ALA495 |
| A | HOH2771 |
| A | HIS468 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1669 |
| Chain | Residue |
| A | HIS420 |
| A | LEU466 |
| A | HIS468 |
| A | SER493 |
| A | HOH2551 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1670 |
| Chain | Residue |
| A | LEU663 |
| A | HOH2762 |
| B | LEU663 |
| B | HOH2736 |
| C | LEU663 |
| C | HOH2728 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PE4 A 1671 |
| Chain | Residue |
| A | ASN340 |
| A | ASN378 |
| A | ASP411 |
| A | TYR412 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PE4 A 1672 |
| Chain | Residue |
| A | GLN98 |
| A | VAL99 |
| A | ASP100 |
| A | TYR101 |
| B | ARG13 |
| B | LEU78 |
| B | HOH2129 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 1667 |
| Chain | Residue |
| B | LEU406 |
| B | ASP407 |
| B | ARG408 |
| B | PRO413 |
| B | ILE414 |
| B | THR415 |
| B | HOH2247 |
| B | HOH2531 |
| B | HOH2540 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1668 |
| Chain | Residue |
| A | LYS186 |
| B | LYS170 |
| B | ALA171 |
| B | PHE194 |
| B | HOH2742 |
| B | HOH2743 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1669 |
| Chain | Residue |
| B | ASN425 |
| B | HOH2744 |
| B | HOH2745 |
| C | ASP210 |
| C | GLN212 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 1670 |
| Chain | Residue |
| B | LEU466 |
| B | HIS468 |
| B | SER493 |
| B | HOH2569 |
| B | HOH2746 |
| B | HOH2747 |
| B | HOH2748 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PE4 B 1671 |
| Chain | Residue |
| B | ASN340 |
| B | ASN378 |
| B | ASP411 |
| B | TYR412 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1672 |
| Chain | Residue |
| A | ARG20 |
| A | SER97 |
| A | HOH2151 |
| B | LYS228 |
| B | HOH2319 |
| B | HOH2750 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 1667 |
| Chain | Residue |
| C | ASP407 |
| C | ARG408 |
| C | PRO413 |
| C | ILE414 |
| C | THR415 |
| C | HOH2733 |
| C | HOH2734 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 1668 |
| Chain | Residue |
| C | TYR417 |
| C | LYS446 |
| C | LYS653 |
| C | ASN655 |
| C | GLU657 |
| C | HOH2505 |
| C | HOH2735 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 1669 |
| Chain | Residue |
| C | THR235 |
| C | VAL236 |
| C | LYS302 |
| C | HOH2736 |
| C | HOH2737 |
| C | HOH2738 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 1670 |
| Chain | Residue |
| C | PRO131 |
| C | ARG148 |
| C | TYR150 |
| C | ASN151 |
| C | HOH2739 |
| C | HOH2740 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL C 1671 |
| Chain | Residue |
| C | HOH2741 |
| C | SER557 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 1672 |
| Chain | Residue |
| C | THR307 |
| C | GLU309 |
| C | LEU337 |
| C | TRP365 |
| C | HOH2742 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PE4 C 1673 |
| Chain | Residue |
| C | ASN340 |
| C | ASN378 |
| C | ASP411 |
| C | TYR412 |
| C | HOH2743 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"8889178","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
