Crystal structure of RV144-elicited antibody CH59 in complex with V2 peptide. Determined by X-ray diffraction at 1.5 Å resolution. Released 6 Feb 2013.
Explore 4HPY in 3D Show helices and sheets RCSB PDB PDBe
4HPY contains 19 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 |
|---|---|---|---|
| β-strand | 3-7 | 5 | 1 |
| β-strand | 11-12 | 2 | 2 |
| β-strand | 18-25 | 8 | 1 |
| β-strand | 34-39 | 6 | 3 |
| β-strand | 45-51 | 7 | 3 |
| β-strand | 57-59 | 3 | 3 |
| β-strand | 67-72 | 6 | 1 |
| α-helix | 73-75 | 3 | |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-94 | 7 | 3 |
| α-helix | 95-96 | 2 | |
| α-helix | 97-99 | 3 | |
| β-strand | 102-103 | 2 | 3 |
| β-strand | 107-109 | 3 | 3 |
| β-strand | 110-111 | 2 | 2 |
| β-strand | 117 | 1 | 4 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 5 |
| α-helix | 128-130 | 3 | |
| β-strand | 131-132 | 2 | 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 | 5 | 1 | 7 |
| β-strand | 9-13 | 4 | 8 |
| α-helix | 18 | 1 | |
| β-strand | 19-24 | 6 | 7 |
| β-strand | 31 | 1 | 9 |
| β-strand | 34-38 | 5 | 8 |
| β-strand | 45-48 | 4 | 8 |
| β-strand | 49 | 1 | 10 |
| β-strand | 53 | 1 | 10 |
| β-strand | 62-67 | 6 | 7 |
| β-strand | 70-75 | 6 | 7 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-91 | 8 | 8 |
| β-strand | 96-98 | 3 | 8 |
| β-strand | 102-106 | 5 | 8 |
| β-strand | 111 | 1 | 11 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 12 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 170 | 1 | 9 |
| α-helix | 174-176 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CH59 Fab heavy chain | H | protein | 225 | Homo sapiens | Q6N089 (AlphaFold model) |
| CH59 Fab light chain | L | protein | 215 | Homo sapiens | Q8N5F4 (AlphaFold model) |
| Envelope glycoprotein gp160 | P | protein | 19 | Human immunodeficiency virus 1 | G9HS63 |
>4HPY_1 CH59 Fab heavy chain (chains H) EVQLVESGGGLVQPGRSLRLSCAASGFTFDDGAMHWVRQAPGKGLEWVSGISWNSNIIAY ADSVKGRFTISRDNAKNSLYLEMNSLRVEDTALYYCAKDSPRGELPLNYWGQGTLVTVSS ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDK
>4HPY_2 CH59 Fab light chain (chains L) DSYELTQPPSVSVSPGQTARITCSGDALPKNYAYWYQQKSGQAPVLVIYEDSKRPSGIPE RFSGSSSGTMATLTISGAQVEDEADYYCYSTDSSGNHRVFGGGTKLTVLGQPKAAPSVTL FPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSY LSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS
>4HPY_3 Envelope glycoprotein gp160 (chains P) ELRDKKQKVHALFYKLDIV
Vaccine Induction of Antibodies against a Structurally Heterogeneous Site of Immune Pressure within HIV-1 Envelope Protein Variable Regions 1 and 2. Liao, H.X., Bonsignori, M., Alam, S.M. et al. Immunity (2013) 38:176-186. DOI 10.1016/j.immuni.2012.11.011 · PubMed
Other PDB entries of the same protein (UniProt Q6N089 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4HPY 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.