1KXB
SINDBIS VIRUS CAPSID (S215A MUTANT), TETRAGONAL CRYSTAL FORM
Functional Information from GO Data
Functional Information from PDB Data
| site_id | TRI |
| Number of Residues | 3 |
| Details | SINDBIS CAPSID PROTEIN HAS THE CATALYTIC TRIAD OF THE SERINE PROTEINASE. THE RESIDUES ARE SER 215, HIS 141, AND ASP 163 IN THE WILD-TYPE. IN THIS MUTANT STRUCTURE, THE ACTIVE SITE SER 215 WAS MUTATED TO ALA TO PREVENT AUTO-CATALYTIC CLEAVAGE BETWEEN TRP 264 AND SER 265. |
| Chain | Residue |
| A | ALA215 |
| A | HIS141 |
| A | ASP163 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027, ECO:0000269|PubMed:1944569 |
| Chain | Residue | Details |
| A | HIS141 | |
| A | ASP163 | |
| A | ALA215 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | SITE: Involved in dimerization of the capsid protein => ECO:0000250|UniProtKB:Q86925 |
| Chain | Residue | Details |
| A | TYR189 | |
| A | ASN222 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | SITE: Cleavage; by autolysis => ECO:0000250|UniProtKB:P03315 |
| Chain | Residue | Details |
| A | TRP264 |
