HIV-1 gp120 Envelope Glycoprotein Complexed with the Broadly Neutralizing CD4-Binding-Site Antibody b12. Determined by X-ray diffraction at 2.3 Å resolution. Released 6 Feb 2007.
Explore 2NY7 in 3D Show helices and sheets RCSB PDB PDBe
2NY7 contains 29 α-helices and 69 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 | 85 | 1 | 1 |
| β-strand | 91-94 | 4 | 2 |
| α-helix | 108-110 | 3 | |
| β-strand | 112-114 | 3 | 3 |
| β-strand | 210-212 | 3 | 3 |
| α-helix | 213-214 | 2 | |
| β-strand | 215 | 1 | 4 |
| β-strand | 218 | 1 | 5 |
| α-helix | 219-220 | 2 | |
| β-strand | 223-228 | 6 | 1 |
| β-strand | 236-239 | 4 | 2 |
| β-strand | 242-245 | 4 | 1 |
| β-strand | 247 | 1 | 5 |
| α-helix | 248-250 | 3 | |
| β-strand | 251 | 1 | 4 |
| β-strand | 256 | 1 | 6 |
| β-strand | 259-261 | 3 | 7 |
| α-helix | 264-266 | 3 | |
| β-strand | 271-273 | 3 | 7 |
| α-helix | 283 | 1 | |
| β-strand | 284-297 | 14 | 7 |
| β-strand | 330-334 | 5 | 7 |
| α-helix | 335-353 | 19 | |
| β-strand | 358-361 | 4 | 7 |
| α-helix | 369-372 | 4 | |
| β-strand | 374-378 | 5 | 6 |
| β-strand | 381-385 | 5 | 6 |
| α-helix | 388-390 | 3 | |
| β-strand | 393-395 | 3 | 7 |
| β-strand | 413-417 | 5 | 7 |
| β-strand | 418-427 | 10 | 6 |
| β-strand | 432-436 | 5 | 6 |
| β-strand | 445-456 | 12 | 7 |
| β-strand | 465-470 | 6 | 7 |
| α-helix | 477-480 | 4 | |
| β-strand | 486-490 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 8 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 9 |
| β-strand | 18-25 | 8 | 8 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 9 |
| α-helix | 44 | 1 | |
| β-strand | 45-51 | 7 | 9 |
| β-strand | 57-59 | 3 | 9 |
| β-strand | 67-72 | 6 | 8 |
| α-helix | 73-75 | 3 | |
| β-strand | 77-82 | 6 | 8 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-94 | 7 | 9 |
| α-helix | 100C | 1 | |
| β-strand | 102-103 | 2 | 9 |
| β-strand | 107-111 | 5 | 9 |
| β-strand | 117 | 1 | 10 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 11 |
| β-strand | 133-134 | 2 | 11 |
| β-strand | 137-147 | 11 | 11 |
| β-strand | 148 | 1 | 10 |
| β-strand | 153-157 | 4 | 12 |
| α-helix | 162-164 | 3 | |
| β-strand | 171-173 | 3 | 11 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-178 | 2 | 11 |
| β-strand | 185-194 | 10 | 11 |
| α-helix | 195-197 | 3 | |
| β-strand | 206-212 | 7 | 12 |
| α-helix | 213-215 | 3 | |
| β-strand | 217-225 | 7 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 13 |
| β-strand | 10-13 | 4 | 14 |
| β-strand | 19-25 | 7 | 13 |
| β-strand | 33-38 | 6 | 14 |
| β-strand | 45-49 | 5 | 14 |
| β-strand | 53-54 | 2 | 14 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 13 |
| β-strand | 70-75 | 6 | 13 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 14 |
| β-strand | 97-98 | 2 | 14 |
| β-strand | 102-106 | 5 | 14 |
| β-strand | 111 | 1 | 15 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 16 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 16 |
| β-strand | 140 | 1 | 15 |
| β-strand | 144-150 | 7 | 17 |
| β-strand | 153-154 | 2 | 17 |
| α-helix | 155 | 1 | |
| β-strand | 159-163 | 5 | 16 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 16 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-198 | 8 | 17 |
| β-strand | 205-210 | 6 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Envelope glycoprotein GP120 | G | protein | 317 | Human immunodeficiency virus 1 | P35961 |
| Antibody b12, heavy chain | H | protein | 230 | Homo sapiens | |
| Antibody b12, light chain | L | protein | 215 | Homo sapiens | P01834 (AlphaFold model) |
>2NY7_1 ENVELOPE GLYCOPROTEIN GP120 (chains G) EVVLVNVTENFNWCKNDMVEQMHEDICSLWDQSLKPCVKLTPLCVGAGSCNTSVITQACP KVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSSQLLLNGSLA EEEVVIRSCNFTDNAKTIIVQLNTSVEINCTGAGHCNIARAKWNNTLKQIASKLREQFGN NKTIIFKQSSGGDPEIVTHWFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTIT LPCRIKQIINMWCKVGKMMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDM RDNWRSELYKYKVVKIE
>2NY7_2 ANTIBODY b12, HEAVY CHAIN (chains H) QVQLVQSGAEVKKPGASVKVSCQASGYRFSNFVIHWVRQAPGQRFEWMGWINPYNGNKEF SAKFQDRVTFTADTSANTAYMELRSLRSADTAVYYCARVGPYSWDDSPQDNYYMDVWGKG TTVIVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTF PAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKAEPKSC
>2NY7_3 ANTIBODY b12, LIGHT CHAIN (chains L) EIVLTQSPGTLSLSPGERATFSCRSSHSIRSRRVAWYQHKPGQAPRLVIHGVSNRASGIS DRFSGSGSGTDFTLTITRVEPEDFALYYCQVYGASSYTFGQGTKLERKRTVAAPSVFIFP PSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL TLSKADYEKHKVYACEVTHQGLRSPVTKSFNRGEC
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 13 |
Structural definition of a conserved neutralization epitope on HIV-1 gp120. Zhou, T., Xu, L., Dey, B. et al. Nature (2007) 445:732-737. DOI 10.1038/nature05580 · PubMed
Other PDB entries of the same protein (UniProt P35961), best resolution first:
MolViewer shows 2NY7 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.