Crystal Structures of the Nipah G Attachment Glycoprotein. Determined by X-ray diffraction at 2.31 Å resolution. Released 19 Aug 2008.
Explore 3D11 in 3D Show helices and sheets RCSB PDB PDBe
3D11 contains 9 α-helices and 35 β-strands across 1 chain. 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 | 178-179 | 2 | 1 |
| α-helix | 185-187 | 3 | |
| β-strand | 201-202 | 2 | 1 |
| α-helix | 204-206 | 3 | |
| β-strand | 215-225 | 11 | 2 |
| β-strand | 228-237 | 10 | 2 |
| 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 | |
| β-strand | 314-320 | 7 | 3 |
| α-helix | 328-331 | 4 | |
| 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 |
| β-strand | 426-430 | 5 | 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 | 571-582 | 12 | 1 |
| β-strand | 587-596 | 10 | 1 |
| α-helix | 597-598 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Hemagglutinin-neuraminidase | A | protein | 428 | Nipah virus | Q9IH62 (AlphaFold model) |
>3D11_1 Hemagglutinin-neuraminidase (chains A) EGVSNLVGLPNNICLQKTSNQILKPKLISYTLPVVGQSGTCITDPLLAMDEGYFAYSHLE RIGSCSRGVSKQRIIGVGEVLDRGDEVPSLFMTNVWTPPNPNTVYHCSAVYNNEFYYVLC AVSTVGDPILNSTYWSGSLMMTRLAVKPKSNGGGYNQHQLALRSIEKGRYDKVMPYGPSG IKQGDTLYFPAVGFLVRTEFKYNDSNCPITKCQYSKPENCRLSMGIRPNSHYILRSGLLK YNLSDGENPKVVFIEISDQRLSIGSPSKIYDSLGQPVFYQASFSWDTMIKFGDVLTVNPL VVNWRNNTVISRPGQSQCPRFNTCPEICWEGVYNDAFLIDRINWISAGVFLDSNQTAENP VFTVFKDNEILYRAQLASEDTNAQKTITNCFLLKNKIWCISLVEIYDTGDNVIRPKLFAV KIPEQCTA
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 1 |
Water and common crystallization additives (IOD) are not listed.
Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Xu, K., Rajashankar, K.R., Chan, Y.P. et al. Proc Natl Acad Sci U S A (2008) 105:9953-9958. DOI 10.1073/pnas.0804797105 · PubMed
Other PDB entries of the same protein (UniProt Q9IH62 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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