7K1O
Crystal Structure of NSP15 Endoribonuclease from SARS CoV-2 in the Complex with Uridine-3',5'-Diphosphate
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue VQV A 401 |
Chain | Residue |
A | HIS235 |
A | GLY247 |
A | GLY248 |
A | HIS250 |
A | LYS290 |
A | TRP333 |
A | THR341 |
A | EDO402 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue EDO A 402 |
Chain | Residue |
A | VAL292 |
A | CYS293 |
A | SER294 |
A | TYR343 |
A | VQV401 |
A | HIS250 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue VQV B 401 |
Chain | Residue |
B | HIS235 |
B | GLY248 |
B | HIS250 |
B | LYS290 |
B | TRP333 |
B | GLU340 |
B | THR341 |
B | EDO402 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO B 402 |
Chain | Residue |
B | HIS250 |
B | LYS290 |
B | VAL292 |
B | SER294 |
B | VQV401 |
site_id | AC5 |
Number of Residues | 10 |
Details | binding site for residue VQV C 401 |
Chain | Residue |
C | HIS235 |
C | GLN245 |
C | GLY247 |
C | GLY248 |
C | HIS250 |
C | LYS290 |
C | TRP333 |
C | GLU340 |
C | THR341 |
C | EDO402 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO C 402 |
Chain | Residue |
C | HIS250 |
C | VAL292 |
C | CYS293 |
C | SER294 |
C | TYR343 |
C | VQV401 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
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 | |
C | HIS235 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
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 | |
C | HIS250 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | ACT_SITE: For uridylate-specific endoribonuclease nsp15 activity => ECO:0000269|PubMed:33504779 |
Chain | Residue | Details |
A | LYS290 | |
B | LYS290 | |
C | LYS290 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093 |
Chain | Residue | Details |
A | LYS290 | |
B | LYS290 | |
C | LYS290 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:33564093 |
Chain | Residue | Details |
A | THR341 | |
B | THR341 | |
C | THR341 |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | SITE: Transition state stabilizer => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093 |
Chain | Residue | Details |
A | LYS290 | |
B | LYS290 | |
C | LYS290 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | SITE: Uracil recognition site => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093 |
Chain | Residue | Details |
A | SER294 | |
B | SER294 | |
C | SER294 |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | SITE: Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3 |
Chain | Residue | Details |
A | GLN347 | |
B | GLN347 | |
C | GLN347 |