Crystal structure of Hendra receptor binding protein head domain in complex with human neutralizing antibody HENV-26. Determined by X-ray diffraction at 2.6 Å resolution. Released 6 Jan 2021.
Explore 6VY6 in 3D Show helices and sheets RCSB PDB PDBe
6VY6 contains 22 α-helices and 79 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 | 201-202 | 2 | 1 |
| α-helix | 204-206 | 3 | |
| β-strand | 215-225 | 11 | 2 |
| β-strand | 228-237 | 10 | 2 |
| α-helix | 243 | 1 | |
| β-strand | 244-257 | 14 | 2 |
| β-strand | 263-271 | 9 | 2 |
| β-strand | 279-287 | 9 | 3 |
| β-strand | 290-297 | 8 | 3 |
| α-helix | 303-306 | 4 | |
| α-helix | 310-312 | 3 | |
| β-strand | 314-320 | 7 | 3 |
| β-strand | 332-337 | 6 | 3 |
| β-strand | 339-341 | 3 | 4 |
| β-strand | 347-350 | 4 | 4 |
| β-strand | 354 | 1 | 3 |
| β-strand | 356-358 | 3 | 4 |
| β-strand | 361-371 | 11 | 4 |
| α-helix | 372-374 | 3 | |
| α-helix | 379-381 | 3 | |
| α-helix | 394-397 | 4 | |
| β-strand | 407-417 | 11 | 4 |
| β-strand | 425-430 | 6 | 4 |
| β-strand | 431 | 1 | 5 |
| α-helix | 432 | 1 | |
| β-strand | 442-447 | 6 | 6 |
| β-strand | 450-455 | 6 | 6 |
| β-strand | 463 | 1 | 7 |
| β-strand | 465-471 | 7 | 6 |
| β-strand | 475 | 1 | 5 |
| β-strand | 476-479 | 4 | 6 |
| β-strand | 486 | 1 | 7 |
| β-strand | 509 | 1 | 1 |
| β-strand | 511-515 | 5 | 8 |
| β-strand | 520-526 | 7 | 8 |
| β-strand | 533 | 1 | 9 |
| β-strand | 535-540 | 6 | 8 |
| β-strand | 545-550 | 6 | 8 |
| β-strand | 557 | 1 | 9 |
| β-strand | 558-568 | 11 | 1 |
| β-strand | 571-580 | 10 | 1 |
| β-strand | 589-596 | 8 | 1 |
| α-helix | 597-598 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 10 |
| β-strand | 10-12 | 3 | 11 |
| β-strand | 18-25 | 8 | 10 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 11 |
| β-strand | 46-51 | 6 | 11 |
| β-strand | 58-60 | 3 | 11 |
| β-strand | 68-73 | 6 | 10 |
| β-strand | 78-83 | 6 | 10 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 11 |
| β-strand | 114-117 | 4 | 11 |
| β-strand | 121-125 | 5 | 11 |
| α-helix | 128-130 | 3 | |
| β-strand | 131 | 1 | 12 |
| α-helix | 132-133 | 2 | |
| β-strand | 134-138 | 5 | 13 |
| β-strand | 149-159 | 11 | 13 |
| β-strand | 160 | 1 | 12 |
| β-strand | 165-168 | 4 | 14 |
| β-strand | 173 | 1 | 14 |
| β-strand | 177-179 | 3 | 13 |
| α-helix | 180-182 | 3 | |
| β-strand | 183-184 | 2 | 13 |
| β-strand | 190-199 | 10 | 13 |
| α-helix | 200-204 | 5 | |
| β-strand | 209-214 | 6 | 14 |
| α-helix | 215-217 | 3 | |
| β-strand | 219-224 | 6 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6 | 1 | 15 |
| β-strand | 10-13 | 4 | 16 |
| β-strand | 19-24 | 6 | 15 |
| α-helix | 28-30 | 3 | |
| β-strand | 34-38 | 5 | 16 |
| β-strand | 45-48 | 4 | 16 |
| β-strand | 49 | 1 | 17 |
| β-strand | 53 | 1 | 17 |
| β-strand | 62-67 | 6 | 15 |
| β-strand | 70-75 | 6 | 15 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-92 | 8 | 16 |
| β-strand | 97-100 | 4 | 16 |
| β-strand | 104-108 | 5 | 16 |
| β-strand | 114 | 1 | 18 |
| α-helix | 115-116 | 2 | |
| β-strand | 117-121 | 5 | 19 |
| α-helix | 125-129 | 5 | |
| β-strand | 133-142 | 10 | 19 |
| β-strand | 143 | 1 | 18 |
| β-strand | 148-153 | 6 | 20 |
| β-strand | 156-158 | 3 | 20 |
| β-strand | 162-164 | 3 | 19 |
| α-helix | 165-167 | 3 | |
| β-strand | 168-169 | 2 | 19 |
| β-strand | 175-183 | 9 | 19 |
| α-helix | 185-189 | 5 | |
| β-strand | 194-200 | 7 | 20 |
| β-strand | 203-209 | 7 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| receptor binding protein | A | protein | 433 | Hendra henipavirus | O89343 (AlphaFold model) |
| Anti-Hendra receptor binding protein antibody HENV-26 Fab heavy chain | H | protein | 230 | Homo sapiens | |
| Anti-Hendra receptor binding protein antibody HENV-26 Fab light chain | L | protein | 214 | Homo sapiens |
>6VY6_1 receptor binding protein (chains A) PNQICLQKTTSTILKPRLISYTLPINTREGVCITDPLLAVDNGFFAYSHLEKIGSCTRGI AKQRIIGVGEVLDRGDKVPSMFMTNVWTPPNPSTIHHCSSTYHEDFYYTLCAVSHVGDPI LNSTSWTESLSLIRLAVRPKSDSGDYNQKYIAITKVERGKYDKVMPYGPSGIKQGDTLYF PAVGFLPRTEFQYNDSNCPIIHCKYSKAENCRLSMGVNSKSHYILRSGLLKYNLSLGGDI ILQFIEIADNRLTIGSPSKIYNSLGQPVFYQASYSWDTMIKLGDVDTVDPLRVQWRNNSV ISRPGQSQCPRFNVCPEVCWEGTYNDAFLIDRLNWVSAGVYLNSNQTAENPVFAVFKDNE ILYQVPLAEDDTNAQKTITDCFLLENVIWCISLVEIYDTGDSVIRPKLFAVKIPAQCSES ENLYFQGHHHHHH
>6VY6_2 Anti-Hendra receptor binding protein antibody HENV-26 Fab heavy chain (chains H) EVQLLESGGGLIQPGGSLRLSCAASGFTFSRFTMSWVRQPPGKGPEWVSGISGSGGHTYY ADSVKGRFTISRDNSKNTLYLQMNSLKAEDTAVYYCAKDGFVGQQLMRRGPWWFDPWGQG TLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTF PAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC
>6VY6_3 Anti-Hendra receptor binding protein antibody HENV-26 Fab light chain (chains L) SYVLTQPPSVSVAPGQTARISCGGNNIGNKGVHWYQQKPGQAPVVVVYDDSDRPSGIPER FSGSNSGNTATLTISRVEAGDEADYYCQVWDSSSDHVVFGGGTKLTVLGQPKANPTVTLF PPSSEELQANKATLVCLISDFYPGAVTVAWKADGSPVKAGVETTKPSKQSNNKYAASSYL SLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS
Water and common crystallization additives (SO4, MPD, CL) are not listed.
Potent Henipavirus Neutralization by Antibodies Recognizing Diverse Sites on Hendra and Nipah Virus Receptor Binding Protein. Dong, J., Cross, R.W., Doyle, M.P. et al. Cell (2020) 183:1536-1550.e17. DOI 10.1016/j.cell.2020.11.023 · PubMed
Other PDB entries of the same protein (UniProt O89343 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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