The crystal structure of IpaH1.4 LRR domain. Determined by X-ray diffraction at 1.4 Å resolution. Released 8 Feb 2023.
Explore 7YA7 in 3D Show helices and sheets RCSB PDB PDBe
7YA7 contains 22 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 | 45-56 | 12 | |
| α-helix | 65-77 | 13 | |
| β-strand | 82-84 | 3 | 1 |
| α-helix | 96-97 | 2 | |
| β-strand | 102-104 | 3 | 1 |
| α-helix | 114-117 | 4 | |
| β-strand | 122-124 | 3 | 1 |
| α-helix | 134-137 | 4 | |
| β-strand | 142-144 | 3 | 1 |
| α-helix | 153-157 | 5 | |
| β-strand | 162-164 | 3 | 1 |
| α-helix | 174-177 | 4 | |
| β-strand | 182-184 | 3 | 1 |
| α-helix | 194-197 | 4 | |
| β-strand | 202-204 | 3 | 1 |
| α-helix | 213-217 | 5 | |
| β-strand | 222-224 | 3 | 1 |
| α-helix | 235-239 | 5 | |
| β-strand | 245-247 | 3 | 1 |
| α-helix | 255-265 | 11 | |
| β-strand | 274-276 | 3 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 48-57 | 10 | |
| α-helix | 65-78 | 14 | |
| β-strand | 82-84 | 3 | 2 |
| α-helix | 95-97 | 3 | |
| β-strand | 102-104 | 3 | 2 |
| α-helix | 115-117 | 3 | |
| β-strand | 122-124 | 3 | 2 |
| α-helix | 135-137 | 3 | |
| β-strand | 142-144 | 3 | 2 |
| α-helix | 153-157 | 5 | |
| β-strand | 162-164 | 3 | 2 |
| α-helix | 174-177 | 4 | |
| β-strand | 182-184 | 3 | 2 |
| α-helix | 195-197 | 3 | |
| β-strand | 202-204 | 3 | 2 |
| α-helix | 213-217 | 5 | |
| β-strand | 222-224 | 3 | 2 |
| α-helix | 235-239 | 5 | |
| β-strand | 245-247 | 3 | 2 |
| α-helix | 255-259 | 5 | |
| β-strand | 274-275 | 2 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RING-type E3 ubiquitin transferase | A, B | protein | 243 | Shigella flexneri 5a | A0A0H2USG1 (AlphaFold model) |
>7YA7_1 RING-type E3 ubiquitin transferase (chains A, B) GPLGSCNEFYLKTWSEWEKNGTPGEQRNIAFNRLKICLQNQEAELNLSELDLKTLPDLPP 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 A0A0H2USG1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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