Molecular mechanisms of viral and host-cell substrate recognition by HCV NS3/4A protease. Determined by X-ray diffraction at 1.6 Å resolution. Released 4 May 2011.
Explore 3RC5 in 3D Show helices and sheets RCSB PDB PDBe
3RC5 contains 8 α-helices and 23 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 992 | 1 | 1 |
| β-strand | 993-999 | 7 | 2 |
| β-strand | 1006-1009 | 4 | 2 |
| α-helix | 1013-1022 | 10 | |
| β-strand | 1024 | 1 | 3 |
| α-helix | 1028-1029 | 2 | |
| β-strand | 1031 | 1 | 4 |
| β-strand | 1033-1037 | 5 | 2 |
| β-strand | 1042-1048 | 7 | 2 |
| β-strand | 1051-1054 | 4 | 2 |
| α-helix | 1056-1059 | 4 | |
| β-strand | 1064 | 1 | 1 |
| β-strand | 1066 | 1 | 3 |
| β-strand | 1071 | 1 | 1 |
| β-strand | 1075-1077 | 3 | 2 |
| β-strand | 1082-1086 | 5 | 2 |
| α-helix | 1087-1088 | 2 | |
| β-strand | 1091 | 1 | 4 |
| β-strand | 1094 | 1 | 2 |
| β-strand | 1096 | 1 | 5 |
| β-strand | 1103-1107 | 5 | 5 |
| α-helix | 1108 | 1 | |
| β-strand | 1113-1118 | 6 | 5 |
| β-strand | 1123-1131 | 9 | 5 |
| α-helix | 1132-1135 | 4 | |
| α-helix | 1141 | 1 | |
| β-strand | 1142-1144 | 3 | 5 |
| β-strand | 1150-1160 | 11 | 5 |
| β-strand | 1163-1171 | 9 | 5 |
| α-helix | 1172-1179 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| NS3/4A protease | A | protein | 203 | Hepatitis C virus subtype 1a | P26664 (AlphaFold model) |
| Product MAVS | B | protein | 8 | Homo sapiens | Q7Z434 (AlphaFold model) |
>3RC5_1 NS3/4A protease (chains A) GSHMASMKKKGSVVIVGRINLSGDTAYAQQTRGEEGCQETSQTGRDKNQVEGEVQIVSTA TQTFLATSINGVLWTVYHGAGTRTIASPKGPVTQMYTNVDKDLVGWQAPQGSRSLTPCTC GSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSAGGPLLCPAGHAVGIFRAAVS TRGVAKAVDFIPVESLETTMRSP
>3RC5_2 Product MAVS (chains B) XQEREVPC
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
Water and common crystallization additives (SO4) are not listed.
Molecular mechanisms of viral and host cell substrate recognition by hepatitis C virus NS3/4A protease. Romano, K.P., Laine, J.M., Deveau, L.M. et al. J Virol (2011) 85:6106-6116. DOI 10.1128/JVI.00377-11 · PubMed
Other PDB entries of the same protein (UniProt P26664 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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