Crystal structure of mouse TLR9 (unliganded form). Determined by X-ray diffraction at 1.96 Å resolution. Released 11 Feb 2015.
Explore 3WPF in 3D Show helices and sheets RCSB PDB PDBe
3WPF contains 23 α-helices and 55 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 | 36-38 | 3 | 1 |
| β-strand | 42-44 | 3 | 1 |
| β-strand | 67-69 | 3 | 1 |
| β-strand | 77-78 | 2 | 2 |
| α-helix | 84-86 | 3 | |
| β-strand | 91-93 | 3 | 1 |
| β-strand | 98 | 1 | 3 |
| β-strand | 113-114 | 2 | 2 |
| β-strand | 127-129 | 3 | 1 |
| β-strand | 133 | 1 | 3 |
| α-helix | 138-140 | 3 | |
| β-strand | 147-149 | 3 | 1 |
| β-strand | 157-158 | 2 | 4 |
| α-helix | 160-163 | 4 | |
| β-strand | 171-173 | 3 | 1 |
| β-strand | 179 | 1 | 5 |
| β-strand | 182 | 1 | 5 |
| β-strand | 189-190 | 2 | 4 |
| β-strand | 203-205 | 3 | 1 |
| α-helix | 214-215 | 2 | |
| β-strand | 224-226 | 3 | 1 |
| β-strand | 234-235 | 2 | 6 |
| α-helix | 237-239 | 3 | |
| β-strand | 248-250 | 3 | 1 |
| β-strand | 256 | 1 | 7 |
| β-strand | 267 | 1 | 7 |
| β-strand | 274-275 | 2 | 6 |
| β-strand | 288-290 | 3 | 1 |
| α-helix | 301-304 | 4 | |
| β-strand | 312-314 | 3 | 1 |
| α-helix | 321-324 | 4 | |
| β-strand | 338-340 | 3 | 1 |
| α-helix | 344-346 | 3 | |
| α-helix | 352-354 | 3 | |
| α-helix | 358-362 | 5 | |
| β-strand | 368-370 | 3 | 1 |
| β-strand | 378-379 | 2 | 8 |
| α-helix | 385-387 | 3 | |
| β-strand | 395-397 | 3 | 1 |
| β-strand | 405-406 | 2 | 8 |
| α-helix | 408-412 | 5 | |
| β-strand | 419-421 | 3 | 1 |
| β-strand | 477-479 | 3 | 1 |
| α-helix | 490-493 | 4 | |
| β-strand | 501-503 | 3 | 1 |
| β-strand | 512 | 1 | 9 |
| β-strand | 526-528 | 3 | 1 |
| β-strand | 535 | 1 | 9 |
| β-strand | 550-552 | 3 | 1 |
| β-strand | 568 | 1 | 10 |
| α-helix | 570-574 | 5 | |
| β-strand | 580-582 | 3 | 1 |
| β-strand | 592 | 1 | 10 |
| β-strand | 597-598 | 2 | 11 |
| β-strand | 603-605 | 3 | 1 |
| α-helix | 611-615 | 5 | |
| β-strand | 627-628 | 2 | 11 |
| β-strand | 633-635 | 3 | 1 |
| α-helix | 646-650 | 5 | |
| β-strand | 658-660 | 3 | 1 |
| α-helix | 671-676 | 6 | |
| β-strand | 682-684 | 3 | 1 |
| β-strand | 693 | 1 | 12 |
| α-helix | 698-699 | 2 | |
| β-strand | 706-708 | 3 | 1 |
| β-strand | 717 | 1 | 12 |
| β-strand | 730-732 | 3 | 1 |
| α-helix | 743-745 | 3 | |
| α-helix | 747-751 | 5 | |
| β-strand | 755-757 | 3 | 1 |
| β-strand | 763-764 | 2 | 13 |
| α-helix | 771-777 | 7 | |
| α-helix | 779-781 | 3 | |
| β-strand | 790 | 1 | 14 |
| β-strand | 791-793 | 3 | 13 |
| β-strand | 798 | 1 | 13 |
| β-strand | 801 | 1 | 14 |
| α-helix | 807-809 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Toll-like receptor 9 | A | protein | 803 | Mus musculus | Q9EQU3 (AlphaFold model) |
>3WPF_1 Toll-like receptor 9 (chains A) RSPWLGTLPAFLPCELKPHGLVDCNWLFLKSVPRFSAAASCSNITRLSLISNRIHHLHNS DFVHLSNLRQLNLKWNCPPTGLSPLHFSCHMTIEPRTFLAMRTLEELNLSYNGITTVPRL PSSLVNLSLSHTNILVLDANSLAGLYSLRVLFMDGNCYYKNPCTGAVKVTPGALLGLSQL THLSLKYNNLTKVPRQLPPSLEYLLVSYNLIVKLGPEDLAQLTSLRVLDVGGNCRRCDHA PNPCIECGQKSLHLHPETFHHLSHLEGLVLKDSSLHTLNSSWFQGLVQLSVLDLSENFLY ESITHTNAFQNLTRLRKLNLSFNYRKKVSFARLHLASSFKNLVSLQELNMNGIFFRLLNK YTLRWLADLPKLHTLHLQMNFINQAQLSIFGTFRALRFVDLSDNRISGPSTLSEATPEEA DDAEQEELLSADPHPAPLSTPASKNFMDRCKNFKFTMDLSRNNLVTIKPEMFVQLSRLQC LSLSHNSIAQAVNGSQFLPLTNLQVLDLSHNKLDLYHWKSFSELPQLQALDLSYNSQPFS MKGIGHQFSFVTHLSMLQSLSLAHNDIHTRVSSHLNSNSVRFLDFSGNGMGRMWDEGGLY LHFFQGLSGLLKLDLSQNNLHILRPQNLDNLPKSLKLLSLRDNYLSFFNWTSLSFLPNLE VLDLAGNQLKALTQGTLPNGTLLQKLDVSSNSIVSVVPAFFALAVELKEVNLSHNILKTV DRSWFGPIVMQLTVLDVRSNPLHCACGAAFVDLLLEVQTKVPGLANGVKCGSPGQLQGRS IFAQDLRLCLDEVLSWDEFLVPR
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 3 |
Water and common crystallization additives (SO4) are not listed.
Structural basis of CpG and inhibitory DNA recognition by Toll-like receptor 9. Ohto, U., Shibata, T., Tanji, H. et al. Nature (2015) 520:702-705. DOI 10.1038/nature14138 · PubMed
Other PDB entries of the same protein (UniProt Q9EQU3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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