9LU3: LN1F9 Fab
LN1F9 Fab bound to Nipah Virus attachment (G) glycoprotein head domain. Determined by X-ray diffraction at 3.0 Å resolution. Released 26 Nov 2025.
- Method
- X-ray diffraction
- Resolution
- 3.0 Å
- Organisms
- Henipavirus nipahense, Mus musculus
- Chains
- 6
- Atoms
- 13,333
- Mol. weight
- 198.64 kDa
- Ligands
- NAG
- Released
- 26 Nov 2025
Explore 9LU3 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9LU3 contains 55 α-helices and 156 β-strands across 6 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.
Chain A: 10 helices, 34 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 178-179 | 2 | 1 |
| α-helix | 185-187 | 3 | |
| β-strand | 201-202 | 2 | 1 |
| α-helix | 204-206 | 3 | |
| β-strand | 216-225 | 10 | 2 |
| β-strand | 228-237 | 10 | 2 |
| β-strand | 244-257 | 14 | 2 |
| β-strand | 263-271 | 9 | 2 |
| α-helix | 276-278 | 3 | |
| β-strand | 279-286 | 8 | 3 |
| β-strand | 290-297 | 8 | 3 |
| α-helix | 307-309 | 3 | |
| β-strand | 314-320 | 7 | 3 |
| α-helix | 328-330 | 3 | |
| β-strand | 332-335 | 4 | 3 |
| β-strand | 340-341 | 2 | 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 |
| α-helix | 424-425 | 2 | |
| β-strand | 426-430 | 5 | 4 |
| β-strand | 431 | 1 | 5 |
| β-strand | 442-447 | 6 | 6 |
| β-strand | 450-455 | 6 | 6 |
| β-strand | 463 | 1 | 7 |
| β-strand | 465-468 | 4 | 6 |
| β-strand | 469-471 | 3 | 8 |
| β-strand | 475 | 1 | 5 |
| β-strand | 476-477 | 2 | 8 |
| β-strand | 486 | 1 | 7 |
| β-strand | 509 | 1 | 1 |
| β-strand | 511-515 | 5 | 9 |
| β-strand | 520-526 | 7 | 9 |
| β-strand | 535-540 | 6 | 9 |
| β-strand | 545-550 | 6 | 9 |
| β-strand | 561-568 | 8 | 1 |
| β-strand | 571-579 | 9 | 1 |
| β-strand | 590-596 | 7 | 1 |
| α-helix | 597-598 | 2 | |
Chain B: 11 helices, 33 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 178-180 | 3 | 21 |
| α-helix | 185-187 | 3 | |
| β-strand | 201-202 | 2 | 21 |
| α-helix | 204-206 | 3 | |
| β-strand | 217-225 | 9 | 22 |
| β-strand | 228-237 | 10 | 22 |
| β-strand | 244-257 | 14 | 22 |
| β-strand | 263-271 | 9 | 22 |
| α-helix | 276-278 | 3 | |
| β-strand | 279-286 | 8 | 23 |
| β-strand | 290-297 | 8 | 23 |
| α-helix | 307-309 | 3 | |
| β-strand | 314-320 | 7 | 23 |
| α-helix | 328-331 | 4 | |
| β-strand | 332-335 | 4 | 23 |
| β-strand | 340-341 | 2 | 24 |
| β-strand | 347-350 | 4 | 24 |
| β-strand | 354 | 1 | 23 |
| β-strand | 356-357 | 2 | 24 |
| β-strand | 361-371 | 11 | 24 |
| α-helix | 372-374 | 3 | |
| α-helix | 379-381 | 3 | |
| α-helix | 394-397 | 4 | |
| β-strand | 407-417 | 11 | 24 |
| α-helix | 424-425 | 2 | |
| β-strand | 426-430 | 5 | 24 |
| β-strand | 431 | 1 | 25 |
| α-helix | 432 | 1 | |
| β-strand | 442-447 | 6 | 26 |
| β-strand | 450-455 | 6 | 26 |
| β-strand | 465-471 | 7 | 26 |
| β-strand | 475 | 1 | 25 |
| β-strand | 476-479 | 4 | 26 |
| β-strand | 509 | 1 | 21 |
| β-strand | 511-515 | 5 | 27 |
| β-strand | 520-526 | 7 | 27 |
| β-strand | 533 | 1 | 28 |
| β-strand | 535-540 | 6 | 27 |
| β-strand | 545-550 | 6 | 27 |
| β-strand | 557 | 1 | 28 |
| β-strand | 561-568 | 8 | 21 |
| β-strand | 571-579 | 9 | 21 |
| β-strand | 590-596 | 7 | 21 |
| α-helix | 597-598 | 2 | |
Chain D: 9 helices, 22 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 29 |
| β-strand | 11-12 | 2 | 30 |
| β-strand | 18-25 | 8 | 29 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 31 |
| β-strand | 45-51 | 7 | 31 |
| β-strand | 57-58 | 2 | 31 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-72 | 6 | 29 |
| β-strand | 77-82 | 6 | 29 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-94 | 7 | 31 |
| β-strand | 102-103 | 2 | 31 |
| β-strand | 107-109 | 3 | 31 |
| β-strand | 110-111 | 2 | 30 |
| β-strand | 117 | 1 | 32 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 33 |
| α-helix | 125-127 | 3 | |
| α-helix | 132-134 | 3 | |
| β-strand | 135-145 | 11 | 33 |
| β-strand | 146 | 1 | 32 |
| β-strand | 151-154 | 4 | 34 |
| α-helix | 155-157 | 3 | |
| β-strand | 163-165 | 3 | 33 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 33 |
| β-strand | 176-185 | 10 | 33 |
| α-helix | 186-188 | 3 | |
| β-strand | 194-200 | 7 | 34 |
| β-strand | 205-211 | 7 | 34 |
Chain E: 8 helices, 22 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 35 |
| β-strand | 10-14 | 5 | 36 |
| β-strand | 19-25 | 7 | 35 |
| β-strand | 33-38 | 6 | 36 |
| β-strand | 45-49 | 5 | 36 |
| β-strand | 53-54 | 2 | 36 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 35 |
| β-strand | 70-75 | 6 | 35 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 36 |
| α-helix | 96 | 1 | |
| β-strand | 97 | 1 | 31 |
| β-strand | 98 | 1 | 36 |
| β-strand | 102-107 | 6 | 36 |
| β-strand | 111 | 1 | 37 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 38 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| β-strand | 129-139 | 11 | 38 |
| β-strand | 140 | 1 | 37 |
| β-strand | 145-150 | 6 | 39 |
| β-strand | 154 | 1 | 39 |
| β-strand | 159-163 | 5 | 38 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 38 |
| α-helix | 183-187 | 5 | |
| β-strand | 192-197 | 6 | 39 |
| β-strand | 205-208 | 4 | 39 |
Chain H: 7 helices, 24 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 10 |
| β-strand | 11-12 | 2 | 11 |
| β-strand | 18-25 | 8 | 10 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 12 |
| β-strand | 45-51 | 7 | 12 |
| β-strand | 57-58 | 2 | 12 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-72 | 6 | 10 |
| β-strand | 77-82 | 6 | 10 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-94 | 7 | 12 |
| β-strand | 102-103 | 2 | 12 |
| β-strand | 107-109 | 3 | 12 |
| β-strand | 110-111 | 2 | 11 |
| β-strand | 117 | 1 | 13 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 14 |
| β-strand | 131-132 | 2 | 14 |
| β-strand | 135-145 | 11 | 14 |
| β-strand | 146 | 1 | 13 |
| β-strand | 151-154 | 4 | 15 |
| α-helix | 155-157 | 3 | |
| β-strand | 159 | 1 | 15 |
| β-strand | 163-165 | 3 | 14 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 14 |
| β-strand | 176-185 | 10 | 14 |
| α-helix | 186-189 | 4 | |
| β-strand | 194-200 | 7 | 15 |
| β-strand | 205-211 | 7 | 15 |
Chain L: 10 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 16 |
| β-strand | 10-14 | 5 | 17 |
| β-strand | 19-25 | 7 | 16 |
| β-strand | 33-38 | 6 | 17 |
| α-helix | 43-44 | 2 | |
| β-strand | 45-49 | 5 | 17 |
| β-strand | 53-54 | 2 | 17 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 16 |
| β-strand | 70-75 | 6 | 16 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 17 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 17 |
| β-strand | 102-107 | 6 | 17 |
| β-strand | 111 | 1 | 18 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 19 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-127 | 6 | |
| β-strand | 129-139 | 11 | 19 |
| β-strand | 140 | 1 | 18 |
| β-strand | 144-150 | 7 | 20 |
| β-strand | 153-154 | 2 | 20 |
| α-helix | 155 | 1 | |
| β-strand | 159-163 | 5 | 19 |
| α-helix | 165-167 | 3 | |
| β-strand | 173-182 | 10 | 19 |
| α-helix | 183-188 | 6 | |
| β-strand | 191-198 | 8 | 20 |
| β-strand | 205-210 | 6 | 20 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Glycoprotein G | A, B | protein | 441 | Henipavirus nipahense | Q9IH62 (AlphaFold model) |
| mAb LN1F9 Fab heavy chain | D, H | protein | 234 | Mus musculus | |
| mAb LN1F9 Fab light chain | E, L | protein | 214 | Mus musculus | |
Sequence of entity 1 (A, B), FASTA
>9LU3_1 Glycoprotein G (chains A, B)
HHHHHHLEVLFQGPEGVSNLVGLPNNICLQKTSNQILKPKLISYTLPVVGQSGTCITDPL
LAMDEGYFAYSHLERIGSCSRGVSKQRIIGVGEVLDRGDEVPSLFMTNVWTPPNPNTVYH
CSAVYNNEFYYVLCAVSTVGDPILNSTYWSGSLMMTRLAVKPKSNGGGYNQHQLALRSIE
KGRYDKVMPYGPSGIKQGDTLYFPAVGFLVRTEFKYNDSNCPITKCQYSKPENCRLSMGI
RPNSHYILRSGLLKYNLSDGENPKVVFIEISDQRLSIGSPSKIYDSLGQPVFYQASFSWD
TMIKFGDVLTVNPLVVNWRNNTVISRPGQSQCPRFNTCPEICWEGVYNDAFLIDRINWIS
AGVFLDSNQTAENPVFTVFKDNEILYRAQLASEDTNAQKTITNCFLLKNKIWCISLVEIY
DTGDNVIRPKLFAVKIPEQCT
Sequence of entity 2 (D, H), FASTA
>9LU3_2 mAb LN1F9 Fab heavy chain (chains D, H)
EVKLVESGGGLVKPGGSLKLSCAASGFSFRNYAMSWVRQSPEKRLEWVAEVSSGGGYTYY
PDTVTGRFTISRDNAKNILYLEMSSLRSEDTAMYYCTRDPDSSGYLAWFAYWGQGTLVTV
SAASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ
SSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHHHHHH
Sequence of entity 3 (E, L), FASTA
>9LU3_3 mAb LN1F9 Fab light chain (chains E, L)
DILLTQSPASLSASVGETVTITCRASENINSYLAWYQQKQGKSPQLLVYNAKTLAEGVPS
RFSGSGSDTQFSLKINTLQPEDFGTYYCQHHSGTPYTFGGGTKLEIKRTVAAPSVFIFPP
SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 10 |
Primary citation
Antigenic landscape of Nipah virus attachment glycoprotein analysis reveals a protective immunodominant epitope across species. Zhou, D., Wang, Y., Yao, Y. et al. NPJ Vaccines (2025) 11:5-5. DOI 10.1038/s41541-025-01319-2 · PubMed
Other PDB entries of the same protein (UniProt Q9IH62 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2VSM 1.8 Å, Nipah virus attachment glycoprotein in complex with human cell surface receptor ephrinB2
- 2VWD 2.25 Å, Nipah Virus Attachment Glycoprotein
- 3D11 2.31 Å, Crystal Structures of the Nipah G Attachment Glycoprotein
- 8JA5 2.79 Å, Crystal structure of Nipah Virus attachment (G) glycoprotein in complex with…
- 8K3C 2.88 Å, Nipah virus Attachment glycoprotein with 41-6 antibody fragment
- 8K0D 2.94 Å, Cryo-EM structure of conformation 2 of complex of Nipah virus attachment G with 1E5…
- 3D12 3.0 Å, Crystal Structures of Nipah Virus G Attachment Glycoprotein in Complex with its Receptor…
- 9LUE 3.03 Å, Cryo-EM structure of the Nipah G head domain in complex with three Fabs
- 8K0C 3.18 Å, Cryo-EM structure of conformation 1 of complex of Nipah virus attachment glycoprotein G…
- 7TXZ 3.2 Å, Nipah Virus attachment (G) glycoprotein ectodomain in complex with nAH1.3 neutralizing…
- 6VY5 3.4 Å, Crystal structure of Nipah receptor binding protein head domain in complex with human…
- 7TY0 3.5 Å, Nipah Virus attachment (G) glycoprotein ectodomain in complex with nAH1.3 neutralizing…
Browse structure collections
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