5YVW
Crystal structure of full length NS3 protein (eD4NS2BNS3) from DENV4 in closed conformation
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue EPE B 701 |
Chain | Residue |
B | LEU193 |
B | GLY414 |
B | ASN416 |
B | GLN456 |
B | ARG460 |
B | ARG463 |
B | HIS194 |
B | PRO195 |
B | GLY196 |
B | ALA197 |
B | GLY198 |
B | LYS199 |
B | GLU285 |
B | ALA316 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU00860 |
Chain | Residue | Details |
B | HIS51 | |
B | ASP75 | |
B | ALA135 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00541 |
Chain | Residue | Details |
B | LEU193 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Involved in NS3 ATPase and RTPase activities => ECO:0000250|UniProtKB:P14335 |
Chain | Residue | Details |
B | ARG457 | |
B | ARG460 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Cleavage; by autolysis => ECO:0000250|UniProtKB:P29990 |
Chain | Residue | Details |
B | LYS618 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine; by host => ECO:0000250|UniProtKB:Q32ZE1 |
Chain | Residue | Details |
B | LYS388 |