Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.4.21.91: Flavivirin

This is an abbreviated version!
For detailed information about Flavivirin, go to the full flat file.

Word Map on EC 3.4.21.91

Reaction

Selective hydrolysis of -Xaa-Xaa-/-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala =

Synonyms

Dengue NS2b-NS3 protease, Dengue NS3 protease, dengue virus non-structural protein 3, dengue virus NS2B-NS3 protease, dengue virus protease, dengue virus serotype 2 protease, DENV NS2B-NS3, DENV-2 NS2B-NS3 protease, DENV2 NS2BNS3pro, DV2 NS2B/NS3pro, flavivirus NS2B-NS3 protease, non-structural protein 3 serine protease, non-structural protein NS2B-NS3 protease, nonstructural protein 3, NS2-3 protease, NS2B-3 proteinase, NS2B-NS3 complex, NS2B-NS3 protease, NS2B-NS3 protease-helicase, NS2B-NS3 proteinase, NS2B-NS3 proteolytic complex, NS2B-NS3 serine protease, NS2B-NS3 serine proteinase, NS2B-NS3(pro)teinase, NS2b-NS3-protease, NS2B-NS3p, NS2B-NS3pro, NS2B/3 protease, NS2B/NS3, NS2B/NS3 complex, NS2B/NS3 protease, NS2B/NS3 protease complex, NS2B/NS3 proteinase, NS2B/NS3 serine protease, NS2B/NS3pro serine protease, NS2B18NS3, NS2BNS3(pro)tease, NS3, NS3 protease, NS3 proteinase, NS3 serine protease, NS3pro, two-component NS2B-NS3 protease, viral serine protease NS2B/NS3, WNV NS2B-NS3, Yellow fever virus (flavivirus) protease, yellow fever virus NS2B-NS3-181 protease, YFV NS2B/NS3 protease, Zika protease, Zika virus NS2B-NS3 protease, ZIKV NS2B/NS3 protease, ZIKV protease

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.91 Flavivirin

Crystallization

Crystallization on EC 3.4.21.91 - Flavivirin

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2.1 A resolution
-
molecular docking of compound 22 shows hydrophobic interactions with Trp50, His51, Arg54, Arg73, Asn74, Asp75, Asn152, and Gly153. The O2 atom of pyrimidine group of compound 22 has two H-bonds, one with the hydroxyl group of Ser135 at 2.76 A and the other with amine group of Asn152 at 2.84 A
-
molecular docking study using flavonoids rom Carica papaya. Highest binding energy is sen with quercetin
-
NS2B-NS3 complex
-
pseudocontact shifts from a lanthanide tag show that NS2Bc remains in the closed conformation also in the complex with bovine pancreatic trypsin inhibitor. The closed conformation is the best template for drug discovery
purified recombinant linked NS2B-NS3pro, X-ray diffraction structure determination and analysis at 1.6 A resolution
-
analysis of enzyme structures, PDB IDs 2FOM, 2M9P, 2M9Q, 2BHR, and 2BMF
analysis of enzyme structures, PDB IDs 3U1I and 3U1J
analysis of enzyme structures, PDB IDs 2JLQ, 2JLR, 2JLU, 2JLV, 2JLW, 2JLX, 2JLY, 2JLZ, 2WHX, 2WZQ, and 2VBC
complete NS3 molecule fused to 18 residues of the NS2B cofactor, by hanging-drop vapor diffusion method, at 3.15 A resolution. Protease domain sits beneath the ATP binding site, giving the molecule an elongated shape. Domain arrangement in the crystal structure fits into an envelope, suggesting a stable molecular conformation. A basic patch located at the surface of the protease domain increases the affinity for nucleotides and may also participate in RNA binding, explaining the higher unwinding activity of the full-length enzyme compared to that of the isolated helicase domain
-
the identification of an alternative stable conformation for the full-length NS2B18NS3 protein is reported. In this second conformation refined to a resolution of 2.2 A, the protease domain has rotated by an angle of 161° relative to the helicase domain
analysis of enzyme structures, PDB IDs 3L6P and 3LKW
by hanging-drop vapour diffusion at 4°C, at 2.3 A resolution. Crystal structure of the catalytic domain of NS2-3 protease, using native and selenomethionine-containing protein yields two crystal forms with the same space group P21. Dimeric cysteine protease with two composite active sites. For each active site, the catalytic histidine and glutamate residues are contributed by one monomer, and the nucleophilic cysteine by the other. Carboxy-terminal residues remain coordinated in the two active sites, predicting an inactive post-cleavage form
-
analysis of enzyme structure, PDB ID 2Z83
analysis of enzyme structures, PDB IDs 2V6I and 2V6J
analysis of enzyme structure, PDB ID 2QEQ
analysis of enzyme structures, PDB IDs 2V8O and 2WV9
analysis of enzyme structures, PDB IDs 2YOL, 3E90, 2FP7, 2IJO, and 2GGV
NS2B-NS3 complex complexed with benzoyl-Nle-Lys-Thr-Arg-H, and trypsin digested NS2B-NS3 complex
-
analysis of enzyme structures, PDB IDs 1YKS and 1YMF
purified bZiPro (C143S)-inhibitor 5-amino-1-((4-methoxyphenyl)sulfonyl)-1H-pyrazol-3-yl benzoate complex and bZiPro (C143S)-Ac-Lys-Arg complex, X-ray diffraction structure determination and analysis at 1.90 A and 1.51 A resolution, respectively
-
purified enzyme complex with bound inhibitor (S)-2-acetamido-6-amino-N-((S)-5-guanidino-1-oxopentan-2-yl)hexanamide, X-ray diffraction structure determination and analysis at 2.4 A resolution
-
purified free NS2B-NS3 protease and complexed with a peptide reversely oriented at the active site, X-ray diffraction structure determination and analysis at 1.58 A resolution. A second protease in the same crystal binds to the residues K14K15G16E17 from the neighboring NS3 in reverse orientation, resisting proteolysis
-
purified NS2B-NS3 protease complexed with the last four amino acids of the NS2B cofactor bound at the NS3 active site, sitting drop vapour diffusion method, mixing of 0.001 ml of 40 mg/ml protein solution with 0.001 ml of reservoir solution containing 0.2 M Na-malonate, pH 4.0, 10% PEG 3350, 18°C, two days, X-ray diffraction structure determination and analysis at 1.84 A resolution
purified ZIKV protease in complex with a peptidomimetic boronic acid inhibitor, X-ray diffraction structure determination and analysis at 2.7 A resolution