The crystal structure of IpaH2.5 LRR domain. Determined by X-ray diffraction at 3.4 Å resolution. Released 8 Feb 2023.
Explore 7YA8 in 3D Show helices and sheets RCSB PDB PDBe
7YA8 contains 13 α-helices and 20 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 | 38-50 | 13 | |
| α-helix | 58-70 | 13 | |
| β-strand | 75-77 | 3 | 1 |
| β-strand | 95-97 | 3 | 1 |
| β-strand | 115-117 | 3 | 1 |
| β-strand | 135-137 | 3 | 1 |
| α-helix | 146-148 | 3 | |
| β-strand | 155-157 | 3 | 1 |
| α-helix | 167-170 | 4 | |
| β-strand | 175-177 | 3 | 1 |
| α-helix | 187-190 | 4 | |
| β-strand | 195-197 | 3 | 1 |
| α-helix | 207-210 | 4 | |
| β-strand | 215-217 | 3 | 1 |
| α-helix | 228-232 | 5 | |
| β-strand | 238-240 | 3 | 1 |
| α-helix | 248-258 | 11 | |
| β-strand | 267-269 | 3 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 34-50 | 17 | |
| α-helix | 58-70 | 13 | |
| β-strand | 75-77 | 3 | 2 |
| β-strand | 95-97 | 3 | 2 |
| β-strand | 115-117 | 3 | 2 |
| β-strand | 135-137 | 3 | 2 |
| β-strand | 155-157 | 3 | 2 |
| α-helix | 167-170 | 4 | |
| β-strand | 175-177 | 3 | 2 |
| β-strand | 195-197 | 3 | 2 |
| β-strand | 215-217 | 3 | 2 |
| α-helix | 228-232 | 5 | |
| β-strand | 238-240 | 3 | 2 |
| α-helix | 248-259 | 12 | |
| β-strand | 267-269 | 3 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RING-type E3 ubiquitin transferase | A, B | protein | 243 | Shigella flexneri 5a | A0A0H2USC0 (AlphaFold model) |
>7YA8_1 RING-type E3 ubiquitin transferase (chains A, B) GPLGSCNEYYLKVWSEWEKNGTPGEQRNIAFNRLKICLQNQEAELNLSELDLKTLPDLPP QITTLEIRKNLLTHLPDLPPMLKVIHAQFNQLESLPALPETLEELNAGDNKIKELPFLPE NLTHLRVHNNRLHILPLLPPELKLLVVSGNRLDSIPPFPDKLEGLALANNFIEQLPELPF SMNRAVLMNNNLTTLPESVLRLAQNAFVNVAGNPLSGHTMRTLQQITTGPDYSGPRIFFS MGN
Structural insight into the recognition of the linear ubiquitin assembly complex by Shigella E3 ligase IpaH1.4/2.5. Hiragi, K., Nishide, A., Takagi, K. et al. J Biochem (2023) 173:317-326. DOI 10.1093/jb/mvac109 · PubMed
Other PDB entries of the same protein (UniProt A0A0H2USC0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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