Structure of the Hepatitis C Envelope Glycoprotein E1 antigenic region 314-324 bound to the cross-neutralizing antibody IGH526. Determined by X-ray diffraction at 1.75 Å resolution. Released 1 Apr 2015.
Explore 4N0Y in 3D Show helices and sheets RCSB PDB PDBe
4N0Y contains 20 α-helices and 49 β-strands across 3 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 |
|---|---|---|---|
| α-helix | 316-323 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-6A | 4 | 1 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 18-25 | 8 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 2 |
| β-strand | 45-51 | 7 | 2 |
| β-strand | 57-59 | 3 | 2 |
| β-strand | 67-72 | 6 | 1 |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 2 |
| β-strand | 98 | 1 | 3 |
| β-strand | 100E | 1 | 3 |
| β-strand | 100H-103 | 4 | 2 |
| β-strand | 107-111 | 5 | 2 |
| α-helix | 114-116 | 3 | |
| β-strand | 117 | 1 | 4 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-127 | 8 | 5 |
| β-strand | 135-145 | 11 | 5 |
| β-strand | 146 | 1 | 4 |
| β-strand | 151-154 | 4 | 6 |
| α-helix | 155-157 | 3 | |
| β-strand | 159 | 1 | 6 |
| β-strand | 163-165 | 3 | 5 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 5 |
| α-helix | 171 | 1 | |
| β-strand | 176-185 | 10 | 5 |
| α-helix | 186-188 | 3 | |
| β-strand | 195-200 | 6 | 6 |
| α-helix | 201-203 | 3 | |
| β-strand | 205-210 | 6 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4 | 1 | 7 |
| β-strand | 5 | 1 | 8 |
| β-strand | 9-13 | 4 | 9 |
| β-strand | 19-24 | 6 | 8 |
| α-helix | 27-29 | 5 | |
| β-strand | 33-38 | 6 | 9 |
| β-strand | 45-48 | 4 | 9 |
| β-strand | 49 | 1 | 10 |
| β-strand | 53 | 1 | 10 |
| α-helix | 54-55 | 2 | |
| β-strand | 62-67 | 6 | 8 |
| β-strand | 70-75 | 6 | 8 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-92 | 9 | 9 |
| β-strand | 95B-98 | 4 | 9 |
| β-strand | 99 | 1 | 7 |
| β-strand | 102-106 | 5 | 9 |
| α-helix | 108-110 | 3 | |
| β-strand | 111 | 1 | 11 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 12 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 130-139 | 10 | 12 |
| β-strand | 140 | 1 | 11 |
| β-strand | 145-150 | 6 | 13 |
| β-strand | 153-155 | 3 | 13 |
| β-strand | 159-161 | 3 | 12 |
| α-helix | 162-164 | 3 | |
| β-strand | 165-166 | 2 | 12 |
| β-strand | 172-180 | 9 | 12 |
| α-helix | 182-187 | 6 | |
| β-strand | 191-197 | 7 | 13 |
| β-strand | 200-206 | 7 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| IGH526 Heavy Chain | H | protein | 231 | Homo sapiens | |
| IGH526 Light Chain | L | protein | 218 | Homo sapiens | |
| HCV E1 peptide | A | protein | 12 | Hepatitis C virus | P27958 (AlphaFold model) |
>4N0Y_1 IGH526 Heavy Chain (chains H) EVQLLEQSGAEVKRPGASVKVSCKASGYTFTSYAIHWVRQAPGQRLEWMGWINPGNGNAK YSQRFQGRVIISRDTSATTSYMELSSLTSEDTAVYSCARDRGFDLLTGHYLGLDPWGQGT LVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFP AVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCGS
>4N0Y_2 IGH526 Light Chain (chains L) EIELTLTQPASASATPGQRVTISCSGSSSNIGGNTVNWYQHLPGAAPKLLIHNNDLRPSG VPDRFSGSKSGTSASLAVSGLQSEDEADYFCAAWDDGLNGWVFGGGTKLTVLGQPKAAPS VTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAA SSYLSLTPEQWKSHKSYSCQVTHEGSTVEKTVAPTECS
>4N0Y_3 HCV E1 peptide (chains A) TGHRMAWDMMMX
Structure of Hepatitis C Virus Envelope Glycoprotein E1 Antigenic Site 314-324 in Complex with Antibody IGH526. Kong, L., Kadam, R.U., Giang, E. et al. J Mol Biol (2015) 427:2617-2628. DOI 10.1016/j.jmb.2015.06.012 · PubMed
Other PDB entries of the same protein (UniProt P27958 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4N0Y directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.