Crystal structure of legAS4 from Legionella pneumophila subsp. pneumophila with histone H3 (3-17)peptide. Determined by X-ray diffraction at 2.22 Å resolution. Released 13 Mar 2024.
Explore 8SR6 in 3D Show helices and sheets RCSB PDB PDBe
8SR6 contains 31 α-helices and 31 β-strands across 2 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 |
|---|---|---|---|
| α-helix | 84-86 | 3 | |
| α-helix | 89-96 | 8 | |
| α-helix | 103-105 | 3 | |
| β-strand | 106 | 1 | 1 |
| β-strand | 117-121 | 5 | 2 |
| α-helix | 123-128 | 6 | |
| β-strand | 131-135 | 5 | 2 |
| β-strand | 139 | 1 | 3 |
| β-strand | 144-147 | 4 | 4 |
| β-strand | 151-154 | 4 | 5 |
| α-helix | 155-164 | 10 | |
| β-strand | 173-176 | 4 | 5 |
| β-strand | 179-182 | 4 | 5 |
| β-strand | 187 | 1 | 1 |
| α-helix | 189-192 | 4 | |
| β-strand | 194-195 | 2 | 4 |
| β-strand | 202-209 | 8 | 4 |
| β-strand | 212-219 | 8 | 4 |
| β-strand | 223 | 1 | 3 |
| α-helix | 227 | 1 | |
| β-strand | 228 | 1 | 2 |
| α-helix | 229 | 1 | |
| β-strand | 230-231 | 2 | 4 |
| β-strand | 236 | 1 | 6 |
| α-helix | 238-243 | 6 | |
| α-helix | 256-262 | 7 | |
| α-helix | 264-266 | 3 | |
| β-strand | 268-271 | 4 | 7 |
| β-strand | 276 | 1 | 8 |
| α-helix | 277-279 | 3 | |
| β-strand | 281 | 1 | 8 |
| β-strand | 286-289 | 4 | 7 |
| α-helix | 291-298 | 8 | |
| α-helix | 302-304 | 3 | |
| α-helix | 310-312 | 3 | |
| α-helix | 315-316 | 2 | |
| β-strand | 317 | 1 | 9 |
| β-strand | 318-319 | 2 | 7 |
| β-strand | 320 | 1 | 10 |
| β-strand | 326 | 1 | 10 |
| α-helix | 327-328 | 2 | |
| β-strand | 335 | 1 | 9 |
| α-helix | 337-344 | 8 | |
| α-helix | 347-355 | 9 | |
| α-helix | 371-380 | 10 | |
| α-helix | 386-397 | 12 | |
| β-strand | 405 | 1 | 11 |
| β-strand | 411 | 1 | 11 |
| α-helix | 412-419 | 8 | |
| α-helix | 422-434 | 13 | |
| α-helix | 441-444 | 4 | |
| β-strand | 446 | 1 | 12 |
| α-helix | 454-460 | 7 | |
| α-helix | 464-473 | 10 | |
| α-helix | 477-482 | 6 | |
| α-helix | 487-500 | 14 | |
| α-helix | 506-517 | 12 | |
| α-helix | 519-521 | 3 | |
| α-helix | 525-531 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5 | 1 | 12 |
| β-strand | 10 | 1 | 6 |
| β-strand | 14 | 1 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Eukaryotic huntingtin interacting protein B | A | protein | 451 | Legionella pneumophila subsp. pneumophila | Q5ZUS4 (AlphaFold model) |
| Histone 3 peptide | B | protein | 15 | Homo sapiens | Q6NXT2 (AlphaFold model) |
>8SR6_1 Eukaryotic huntingtin interacting protein B (chains A) NADEWIDTSKIMLDLHIDNMSSSDYIPSAIDRTDLVMVQSVHLLRKTGGRGLFAREDIPK GTCIGIYTGEVYSEQEFEQYLKEHVGSDKSYAMYVGGRVIDAARKGNLTRYINFSDSQDN AEFVETTLNRKKVAKVITTKNIKAGQQLLINYNTYEEQASRYYYFLNPGDGWLSAQEFYQ TYQSQYRLEQMPYNLEGFDLKAGDRVLMTQIGRIILANYSLAKEQELNASDIDLPFLKVG SDEKILDFDEADTFTPLMAACYLGQVENVKWLIEHGANIDQQQSHSGHCPLSLTLKGYSL AKDTQKYIDIIQLLIKNQVNLLVHDRSDKTFLHNAALVLNNLDFQSVVKFLIGQNPIDIN EYFTYIDENDFDIVMHCYNNKLFDKALVLLAFYPDYFKRNYMSDNEGHNQFNINAFRKAI KDFNSNERSILLMQLRESGLHLPEDLLEQLG
>8SR6_2 Histone 3 peptide (chains B) TKQTARKSTGGKAPR
| ID | Name | Formula | Copies |
|---|---|---|---|
| SAH | S-adenosyl-L-homocysteine | C14 H20 N6 O5 S | 1 |
Water and common crystallization additives (K, EDO, PEG, GOL) are not listed.
The SET and ankyrin domains of the secreted Legionella pneumophila histone methyltransferase work together to modify host chromatin. Rolando, M., Wah Chung, I.Y., Xu, C. et al. mBio (2023) 14:e0165523-e0165523. DOI 10.1128/mbio.01655-23 · PubMed
Other PDB entries of the same protein (UniProt Q5ZUS4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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