Cryo-EM structure of EBV gp350 D123 in complex with neutralizing antibody 4A11. Determined by electron microscopy at 3.33 Å resolution. Released 18 Mar 2026.
Explore 9MA0 in 3D Show helices and sheets RCSB PDB PDBe
9MA0 contains 6 α-helices and 60 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 | 2-6 | 5 | 1 |
| β-strand | 10 | 1 | 2 |
| β-strand | 16-21 | 6 | 3 |
| β-strand | 38-44 | 7 | 1 |
| β-strand | 49-55 | 7 | 1 |
| β-strand | 67 | 1 | 3 |
| β-strand | 83-89 | 7 | 3 |
| β-strand | 92-98 | 7 | 3 |
| β-strand | 114-124 | 11 | 1 |
| β-strand | 130-143 | 14 | 1 |
| β-strand | 163-165 | 3 | 4 |
| β-strand | 170-171 | 2 | 4 |
| β-strand | 172-178 | 7 | 5 |
| β-strand | 186 | 1 | 6 |
| β-strand | 188-194 | 7 | 4 |
| β-strand | 199-203 | 5 | 4 |
| β-strand | 216-220 | 5 | 5 |
| β-strand | 222-223 | 2 | 4 |
| β-strand | 225 | 1 | 2 |
| β-strand | 233-238 | 6 | 5 |
| β-strand | 251-258 | 8 | 5 |
| β-strand | 270-271 | 2 | 4 |
| β-strand | 274-277 | 4 | 4 |
| β-strand | 279 | 1 | 6 |
| β-strand | 288-290 | 3 | 4 |
| β-strand | 293-296 | 4 | 4 |
| α-helix | 306-307 | 2 | |
| β-strand | 310-314 | 5 | 7 |
| β-strand | 316 | 1 | 8 |
| β-strand | 319-324 | 6 | 8 |
| β-strand | 338-343 | 6 | 7 |
| β-strand | 357-358 | 2 | 7 |
| α-helix | 363-364 | 2 | |
| β-strand | 370-373 | 4 | 8 |
| β-strand | 380-385 | 6 | 8 |
| β-strand | 394-398 | 5 | 7 |
| β-strand | 406-413 | 8 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-6 | 2 | 9 |
| β-strand | 10-11 | 2 | 10 |
| β-strand | 18-23 | 6 | 9 |
| α-helix | 30-32 | 3 | |
| β-strand | 37-38 | 2 | 11 |
| β-strand | 39 | 1 | 12 |
| β-strand | 41 | 1 | 13 |
| β-strand | 43 | 1 | 13 |
| β-strand | 46-47 | 2 | 11 |
| α-helix | 70-72 | 3 | |
| β-strand | 80-85 | 6 | 9 |
| β-strand | 93 | 1 | 12 |
| β-strand | 100 | 1 | 14 |
| β-strand | 111 | 1 | 14 |
| α-helix | 112-113 | 2 | |
| β-strand | 121 | 1 | 12 |
| β-strand | 122-123 | 2 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-5 | 2 | |
| β-strand | 10 | 1 | 15 |
| β-strand | 13 | 1 | 16 |
| β-strand | 19 | 1 | 17 |
| β-strand | 39-43 | 5 | 15 |
| β-strand | 49-51 | 3 | 15 |
| β-strand | 67 | 1 | 17 |
| β-strand | 80 | 1 | 17 |
| β-strand | 89-94 | 6 | 15 |
| β-strand | 103 | 1 | 15 |
| β-strand | 107-109 | 3 | 15 |
| β-strand | 111 | 1 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Envelope glycoprotein GP350 | A | protein | 478 | Human herpesvirus 4 strain B95-8 | P03200 (AlphaFold model) |
| 4A11 heavy chain | B | protein | 248 | Homo sapiens | |
| 4A11 light chain | C | protein | 237 | Homo sapiens |
>9MA0_1 Envelope glycoprotein GP350 (chains A) MEAALLVCQYTIQSLIHLTGEDPGFFNVEIPEFPFYPTCNVCTADVNVTINFDVGGKKHQ LDLDFGQLTPHTKAVYQPRGAFGGSENATNLFLLELLGAGELALTMRSKKLPINVTTGEE QQVSLESVDVYFQDVFGTMWCHHAEMQNPVYLIPETVPYIKWDNCNSTNITAVVRAQGLD VTLPLSLPTSAQDSNFSVKTQMLGNEIDIECIMEDGEISQVLPGDNKFNITCSGYESHVP SGGILTSTSPVATPIPGTGYAYSLRLTPRPVSRFLGNNSILYVFYSGNGPKASGGDYCIQ SNIVFSDEIPASQDMPTNTTDITYVGDNATYSVPMVTSEDANSPNVTVTAFWAWPNNTET DFKCKWTLTSGTPSGCENISGAFASNRTFDITVSGLGTAPKTLIITRTATNATTTTHKVI FSKAPESTTTSPTLNTTGFADPNTTTGLPSSTHVPTNLTAPASTGPTVSTGSHHHHHH
>9MA0_2 4A11 heavy chain (chains B) MGWSCIILFLVATATGVHSQVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYIHWVRQAP GQGLEWMGWMNPNSGATNYAQKFQGRVTMTRDTSINTAYMELSSLRSDDTAVYFCAKDPR YSSSWRHNWFDPWGQGTLVSVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPV TVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKR VEPKSCDK
>9MA0_3 4A11 light chain (chains C) MGWSCIILFLVATATGSWADIVLTQSPLSLTVTPGEPASISCRSSQSLLHSSGHNFLSWY LQKPGQSPQLLIYLGSNRASGVPDRFSGSGTGADFTLKISRVEAEDVGVYYCLQTLRAPF TFGQGTRLEIKGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPV KAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS
Cryo-EM structure of EBV gp350 D123 in complex with neutralizing antibody 4A11. Ma, H.Y., Sun, C. To be published.
Other PDB entries of the same protein (UniProt P03200 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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