6VWW
Crystal Structure of NSP15 Endoribonuclease from SARS CoV-2.
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue GOL A 401 |
Chain | Residue |
A | LEU43 |
A | PHE44 |
A | GLU45 |
A | GLU267 |
A | HOH623 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue GOL A 402 |
Chain | Residue |
A | GLY147 |
A | GLY126 |
A | ARG127 |
A | THR145 |
A | GLU146 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue MG A 403 |
Chain | Residue |
A | SER262 |
A | PRO263 |
A | ASP283 |
A | ALA284 |
A | GLN285 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue GOL A 404 |
Chain | Residue |
A | GLY77 |
A | ASP79 |
A | PRO119 |
A | HOH518 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue GOL A 405 |
Chain | Residue |
A | GLU69 |
A | LYS90 |
A | THR167 |
A | SER198 |
A | ASN200 |
A | HOH542 |
A | HOH547 |
A | HOH555 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue ACY A 406 |
Chain | Residue |
A | ASN200 |
A | LEU201 |
A | TYR279 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue GOL B 401 |
Chain | Residue |
B | ASN75 |
B | SER274 |
B | THR275 |
B | VAL276 |
B | HOH530 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue GOL B 402 |
Chain | Residue |
B | LYS90 |
B | THR167 |
B | SER198 |
B | ARG199 |
B | ASN200 |
B | HOH501 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue GOL B 403 |
Chain | Residue |
B | GLY77 |
B | ASP79 |
B | PRO119 |
B | THR121 |
B | HOH509 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue CL B 404 |
Chain | Residue |
A | THR322 |
B | VAL149 |
B | GLY151 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue GOL B 405 |
Chain | Residue |
B | LEU43 |
B | PHE44 |
B | GLU45 |
B | TRP59 |
B | HOH513 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue GOL B 406 |
Chain | Residue |
B | GLU192 |
B | LYS320 |
B | THR322 |
B | GLU327 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue ACY B 407 |
Chain | Residue |
B | GLU146 |
B | LYS174 |
B | GLN176 |
B | PHE177 |
B | ASN178 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for residue ACY B 408 |
Chain | Residue |
B | LEU312 |
B | SER313 |
B | VAL314 |
B | VAL315 |
B | CYS334 |
B | LYS335 |
B | ASP336 |
B | GLY337 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor; for uridylate-specific endoribonuclease nsp15 activity => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093 |
Chain | Residue | Details |
A | HIS235 | |
B | HIS235 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor; for uridylate-specific endoribonuclease nsp15 activity => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093 |
Chain | Residue | Details |
A | HIS250 | |
B | HIS250 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | ACT_SITE: For uridylate-specific endoribonuclease nsp15 activity => ECO:0000269|PubMed:33504779 |
Chain | Residue | Details |
A | LYS290 | |
B | LYS290 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093 |
Chain | Residue | Details |
A | LYS290 | |
B | LYS290 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:33564093 |
Chain | Residue | Details |
A | THR341 | |
B | THR341 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093 |
Chain | Residue | Details |
A | LYS290 | |
B | LYS290 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | SITE: Uracil recognition site => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093 |
Chain | Residue | Details |
A | SER294 | |
B | SER294 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | SITE: Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3 |
Chain | Residue | Details |
A | GLN347 | |
B | GLN347 |