Crystal structure of a complex between Bacillus subtilis flagellin and zebrafish Toll-like receptor 5. Determined by X-ray diffraction at 2.1 Å resolution. Released 15 Feb 2017.
Explore 5GY2 in 3D Show helices and sheets RCSB PDB PDBe
5GY2 contains 28 α-helices and 74 β-strands across 4 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 | 26-28 | 3 | 1 |
| β-strand | 31-33 | 3 | 1 |
| α-helix | 42-44 | 3 | |
| β-strand | 51-53 | 3 | 1 |
| β-strand | 61-62 | 2 | 2 |
| β-strand | 75-77 | 3 | 1 |
| β-strand | 86-87 | 2 | 2 |
| β-strand | 100-102 | 3 | 1 |
| β-strand | 110-111 | 2 | 2 |
| β-strand | 124-126 | 3 | 1 |
| β-strand | 133 | 1 | 3 |
| α-helix | 135-138 | 4 | |
| β-strand | 150-152 | 3 | 1 |
| β-strand | 157 | 1 | 3 |
| α-helix | 165-169 | 5 | |
| β-strand | 175-177 | 3 | 1 |
| β-strand | 183 | 1 | 4 |
| α-helix | 192-194 | 3 | |
| β-strand | 198-203 | 6 | 1 |
| β-strand | 208 | 1 | 4 |
| α-helix | 217-220 | 4 | |
| β-strand | 230-235 | 6 | 1 |
| α-helix | 243-252 | 10 | |
| β-strand | 257-262 | 6 | 1 |
| α-helix | 279-281 | 3 | |
| α-helix | 287-291 | 5 | |
| β-strand | 296-298 | 3 | 1 |
| β-strand | 306-307 | 2 | 5 |
| β-strand | 320-322 | 3 | 1 |
| β-strand | 330-331 | 2 | 5 |
| β-strand | 344-346 | 3 | 1 |
| β-strand | 355 | 1 | 6 |
| β-strand | 368-370 | 3 | 1 |
| β-strand | 379 | 1 | 6 |
| β-strand | 392-394 | 3 | 1 |
| β-strand | 416-418 | 3 | 1 |
| β-strand | 424 | 1 | 7 |
| α-helix | 432-440 | 9 | |
| β-strand | 445 | 1 | 1 |
| β-strand | 450 | 1 | 8 |
| β-strand | 451 | 1 | 7 |
| β-strand | 457 | 1 | 8 |
| α-helix | 458-460 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 26-28 | 3 | 11 |
| β-strand | 31-33 | 3 | 11 |
| α-helix | 42-44 | 3 | |
| β-strand | 51-53 | 3 | 11 |
| β-strand | 61-62 | 2 | 12 |
| β-strand | 75-77 | 3 | 11 |
| β-strand | 86-87 | 2 | 12 |
| β-strand | 100-102 | 3 | 11 |
| β-strand | 110-111 | 2 | 12 |
| β-strand | 124-126 | 3 | 11 |
| β-strand | 133 | 1 | 13 |
| α-helix | 135-138 | 4 | |
| β-strand | 150-152 | 3 | 11 |
| β-strand | 157 | 1 | 13 |
| α-helix | 165-169 | 5 | |
| β-strand | 175-177 | 3 | 11 |
| β-strand | 183 | 1 | 14 |
| α-helix | 192-194 | 3 | |
| β-strand | 198-203 | 6 | 11 |
| β-strand | 208 | 1 | 14 |
| α-helix | 217-221 | 5 | |
| β-strand | 230-235 | 6 | 11 |
| α-helix | 243-252 | 10 | |
| β-strand | 257-262 | 6 | 11 |
| α-helix | 279-281 | 3 | |
| α-helix | 287-291 | 5 | |
| β-strand | 296-298 | 3 | 11 |
| β-strand | 306-307 | 2 | 15 |
| β-strand | 320-322 | 3 | 11 |
| β-strand | 330-331 | 2 | 15 |
| β-strand | 344-346 | 3 | 11 |
| β-strand | 355 | 1 | 16 |
| β-strand | 368-370 | 3 | 11 |
| β-strand | 379 | 1 | 16 |
| β-strand | 392-394 | 3 | 11 |
| β-strand | 416-418 | 3 | 11 |
| β-strand | 424 | 1 | 17 |
| α-helix | 432-440 | 9 | |
| β-strand | 445 | 1 | 11 |
| β-strand | 450 | 1 | 18 |
| β-strand | 451 | 1 | 17 |
| β-strand | 457 | 1 | 18 |
| α-helix | 458-460 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 55-98 | 44 | |
| α-helix | 107-128 | 22 | |
| β-strand | 130-131 | 2 | 9 |
| β-strand | 134-135 | 2 | 9 |
| β-strand | 146-149 | 4 | 10 |
| β-strand | 157-160 | 4 | 10 |
| α-helix | 167-170 | 4 | |
| α-helix | 185-221 | 37 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tlr5b protein,Variable lymphocyte receptor B | A, B | protein | 455 | Danio rerio, Eptatretus burgeri | B3DIN1 (AlphaFold model), Q4G1L2 (AlphaFold model) |
| Flagellin | C, D | protein | 183 | Bacillus subtilis subsp. spizizenii strain W23 | E0U497 (AlphaFold model) |
>5GY2_1 Tlr5b protein,Variable lymphocyte receptor B (chains A, B) ADPGTSECSVIGYNAICINRGLHQVPELPAHVNYVDLSLNSIAELNETSFSRLQDLQFLK VEQQTPGLVIRNNTFRGLSSLIILKLDYNQFLQLETGAFNGLANLEVLTLTQCNLDGAVL SGNFFKPLTSLEMLVLRDNNIKKIQPASFFLNMRRFHVLDLTFNKVKSICEEDLLNFQGK HFTLLRLSSITLQDMNEYWLGWEKCGNPFKNTSITTLDLSGNGFKESMAKRFFDAIAGTK IQSLILSNSYNMGSSFGHTNFKDPDNFTFKGLEASGVKTCDLSKSKIFALLKSVFSHFTD LEQLTLAQNEINKIDDNAFWGLTHLLKLNLSQNFLGSIDSRMFENLDKLEVLDLSYNHIR ALGDQSFLGLPNLKELALDTNQLKSVPDGIFDRLTSLQKIWLHTNPWDCSCPRIDYLSRW LNKNSQKEQGSAKCSGSGKPVRSIICPTSASLVPR
>5GY2_2 Flagellin (chains C, D) GSAKDPGQIRGLEMASKNSQDGISLIQTAEGALTETHAILQRMRELTVQAGNTGTQQAED LGAIKDEMDALIEEIDGISNRTEFNGKKLLDGTNSTDGFTFQIGANAGQQLNVKIDSMSS TALGVNALDVTDFAATAFDDQLKSIDTAINTVSTQRAKLGAVQNRLEHTINNLGASGENL TAA
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 6 |
Water and common crystallization additives (PG4) are not listed.
A conserved TLR5 binding and activation hot spot on flagellin. Song, W.S., Jeon, Y.J., Namgung, B. et al. Sci Rep (2017) 7:40878-40878. DOI 10.1038/srep40878 · PubMed
Other PDB entries of the same protein (UniProt B3DIN1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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