Neutralization of dengue virus by a serotype cross-reactive antibody elucidated by cryoelectron microscopy and x-ray crystallography. Determined by X-ray diffraction at 3.0 Å resolution. Released 25 Dec 2007.
Explore 2R29 in 3D Show helices and sheets RCSB PDB PDBe
2R29 contains 9 α-helices and 61 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 | 301 | 1 | 1 |
| α-helix | 302 | 1 | |
| β-strand | 305-314 | 10 | 2 |
| β-strand | 320-327 | 8 | 2 |
| β-strand | 334 | 1 | 1 |
| β-strand | 337 | 1 | 3 |
| β-strand | 340 | 1 | 4 |
| β-strand | 350-351 | 2 | 2 |
| α-helix | 364 | 1 | |
| β-strand | 365-366 | 2 | 2 |
| β-strand | 369-370 | 2 | 2 |
| β-strand | 377 | 1 | 4 |
| β-strand | 380 | 1 | 3 |
| β-strand | 387 | 1 | 3 |
| β-strand | 390 | 1 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-12 | 2 | 5 |
| β-strand | 18-23 | 6 | 6 |
| β-strand | 34-39 | 6 | 7 |
| β-strand | 46-51 | 6 | 7 |
| β-strand | 59-60 | 2 | 7 |
| α-helix | 62-64 | 3 | |
| β-strand | 70 | 1 | 6 |
| β-strand | 73 | 1 | 6 |
| β-strand | 78-83 | 6 | 6 |
| β-strand | 92-95 | 4 | 7 |
| β-strand | 110-112 | 3 | 7 |
| β-strand | 113-114 | 2 | 5 |
| α-helix | 118-119 | 2 | |
| β-strand | 124-127 | 4 | 8 |
| β-strand | 141 | 1 | 9 |
| β-strand | 142-148 | 7 | 8 |
| β-strand | 154-156 | 3 | 10 |
| β-strand | 166 | 1 | 9 |
| β-strand | 169 | 1 | 8 |
| β-strand | 178-181 | 4 | 8 |
| β-strand | 184 | 1 | 9 |
| β-strand | 197-202 | 6 | 10 |
| α-helix | 203-205 | 3 | |
| β-strand | 207-212 | 6 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6 | 1 | 11 |
| β-strand | 12-13 | 2 | 12 |
| β-strand | 19-21 | 3 | 13 |
| β-strand | 23 | 1 | 11 |
| β-strand | 30 | 1 | 14 |
| β-strand | 35 | 1 | 14 |
| β-strand | 37-42 | 6 | 15 |
| β-strand | 50 | 1 | 15 |
| β-strand | 52 | 1 | 16 |
| α-helix | 57 | 1 | |
| β-strand | 58 | 1 | 16 |
| α-helix | 59 | 1 | |
| β-strand | 67-70 | 4 | 13 |
| β-strand | 75-79 | 5 | 13 |
| β-strand | 89-94 | 6 | 15 |
| β-strand | 102 | 1 | 15 |
| β-strand | 106-107 | 2 | 15 |
| β-strand | 109-110 | 2 | 12 |
| α-helix | 114-115 | 2 | |
| β-strand | 122 | 1 | 17 |
| α-helix | 123-125 | 3 | |
| β-strand | 133 | 1 | 18 |
| β-strand | 136-137 | 2 | 17 |
| β-strand | 143 | 1 | 19 |
| β-strand | 151 | 1 | 20 |
| β-strand | 163-167 | 5 | 17 |
| β-strand | 177 | 1 | 19 |
| β-strand | 179-183 | 5 | 17 |
| β-strand | 186 | 1 | 18 |
| β-strand | 195-200 | 6 | 20 |
| β-strand | 205-210 | 6 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Envelope protein E | A | protein | 97 | Dengue virus 2 Thailand/16681/84 | P29991 |
| Heavy chain of Fab 1A1D-2 | H | protein | 216 | Mus musculus | P01863 (AlphaFold model) |
| Light chain of Fab 1A1D-2 | L | protein | 217 | Mus musculus | P01660 (AlphaFold model) |
>2R29_1 Envelope protein E (chains A) SYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPI VTEKDSPVNIEAEPPFGDSYIIIGVEPGQLKLNWFKK
>2R29_2 Heavy chain of Fab 1A1D-2 (chains H) EVQLQQSGAELVKPGASVKLSCTASGFNIKDTYMHWVKQRPEQGLEWIGRIDPANGYSKY DPKFQGKATITADTSSNAAYLQLSSLTSEDTAVYFCARDYEGFAYWGQGTLVTVSSAKTT PPSVYPLAPGAAAATSSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTL SSSVTVTSSTWPSQTITCNVAHPASSTKVDKKIEPR
>2R29_3 Light chain of Fab 1A1D-2 (chains L) DIVLTQSPASLAVSLGQRATISCRASESVVRYGNSFMHWYQQKPGQPPKLLIYRASSLES GIPTRFSGSGSRTDFTLTINPVEADDVATYYCQQTNVDPWAFGGGTKLEIKRADAAPTVS IFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMS STLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNE
Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins. Lok, S.M., Kostyuchenko, V., Nybakken, G.E. et al. Nat Struct Mol Biol (2008) 15:312-317. DOI 10.1038/nsmb.1382 · PubMed
Other PDB entries of the same protein (UniProt P29991), best resolution first:
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