Crystal structure of broadly neutralizing anti-HIV-1 antibody 4E10, mutant Npro, with peptide bound. Determined by X-ray diffraction at 1.49 Å resolution. Released 5 Apr 2017.
Explore 5X08 in 3D Show helices and sheets RCSB PDB PDBe
5X08 contains 20 α-helices and 44 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 | 3-6 | 4 | 1 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 18-25 | 8 | 1 |
| β-strand | 34-39 | 6 | 2 |
| β-strand | 45-52 | 8 | 2 |
| α-helix | 52A-54 | 3 | |
| β-strand | 56-59 | 4 | 2 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-72 | 6 | 1 |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-97 | 10 | 2 |
| β-strand | 100F-103 | 8 | 2 |
| β-strand | 107-111 | 5 | 2 |
| β-strand | 117 | 1 | 3 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 4 |
| β-strand | 137-147 | 11 | 4 |
| β-strand | 148 | 1 | 3 |
| β-strand | 153-157 | 4 | 5 |
| α-helix | 162-164 | 3 | |
| β-strand | 166 | 1 | 5 |
| β-strand | 171-173 | 3 | 4 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-178 | 2 | 4 |
| β-strand | 185-194 | 10 | 4 |
| α-helix | 195-198 | 4 | |
| β-strand | 207-212 | 6 | 5 |
| α-helix | 213-215 | 3 | |
| β-strand | 217-222 | 6 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-5 | 2 | 6 |
| β-strand | 10-13 | 4 | 7 |
| β-strand | 19-25 | 7 | 6 |
| α-helix | 27A-28 | 2 | |
| α-helix | 29-31 | 3 | |
| β-strand | 33-38 | 6 | 7 |
| β-strand | 45-48 | 4 | 7 |
| β-strand | 49 | 1 | 8 |
| β-strand | 53 | 1 | 8 |
| β-strand | 62-67 | 6 | 6 |
| β-strand | 70-75 | 6 | 6 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 7 |
| β-strand | 97-98 | 2 | 7 |
| β-strand | 102-106 | 5 | 7 |
| β-strand | 111 | 1 | 9 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 10 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 10 |
| β-strand | 140 | 1 | 9 |
| β-strand | 145-150 | 6 | 11 |
| β-strand | 153-154 | 2 | 11 |
| α-helix | 155 | 1 | |
| β-strand | 159-163 | 5 | 10 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 10 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-197 | 7 | 11 |
| β-strand | 205-210 | 6 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 672-674 | 3 | |
| α-helix | 675-683 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fab 4E10 Heavy chain | H | protein | 230 | Homo sapiens | |
| Fab 4E10 Light chain | L | protein | 214 | Homo sapiens | |
| Envelope glycoprotein gp160 | P | protein | 16 | Human immunodeficiency virus type 1 (MAL ISOLATE) | P04578 (AlphaFold model) |
>5X08_1 Fab 4E10 Heavy chain (chains H) QVQLVQSGAEVKRPGSSVTVSCKASGGSFSTYALSWVRQAPGRGLEWMGGVIPLLTITNY APRFQGRITITADRSTSTAYLELNSLRPEDTAVYYCAREGTTPPGWGWLGKPIGAFAHWG QGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVH TFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPK
>5X08_2 Fab 4E10 Light chain (chains L) EIVLTQSPGTQSLSPGERATLSCRASQSVGNNKLAWYQQRPGQAPRLLIYGASSRPSGVA DRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGQSLSTFGQGTKVEVKRTVAAPSVFIFP PSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGE
>5X08_3 Envelope glycoprotein gp160 (chains P) NWFDITNWLWYIKKKK
Functional Contacts between MPER and the Anti-HIV-1 Broadly Neutralizing Antibody 4E10 Extend into the Core of the Membrane. Rujas, E., Insausti, S., Garcia-Porras, M. et al. J Mol Biol (2017) 429:1213-1226. DOI 10.1016/j.jmb.2017.03.008 · PubMed
Other PDB entries of the same protein (UniProt P04578 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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