Crystal structure of IpaH1.4 LRR domain bound to HOIL-1L UBL domain. Determined by X-ray diffraction at 1.9 Å resolution. Released 30 Mar 2022.
Explore 7V8E in 3D Show helices and sheets RCSB PDB PDBe
7V8E contains 28 α-helices and 34 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 |
|---|---|---|---|
| α-helix | 37-50 | 14 | |
| α-helix | 58-70 | 13 | |
| β-strand | 75-77 | 3 | 4 |
| α-helix | 88-90 | 3 | |
| β-strand | 95-97 | 3 | 4 |
| α-helix | 108-110 | 3 | |
| β-strand | 115-117 | 3 | 4 |
| α-helix | 128-130 | 3 | |
| β-strand | 135-137 | 3 | 4 |
| β-strand | 155-157 | 3 | 4 |
| α-helix | 167-170 | 4 | |
| β-strand | 175-177 | 3 | 4 |
| α-helix | 187-190 | 4 | |
| β-strand | 195-197 | 3 | 4 |
| α-helix | 207-210 | 4 | |
| β-strand | 215-217 | 3 | 4 |
| α-helix | 228-232 | 5 | |
| β-strand | 238-240 | 3 | 4 |
| α-helix | 248-258 | 11 | |
| β-strand | 267-269 | 3 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 37-49 | 13 | |
| α-helix | 58-70 | 13 | |
| β-strand | 75-77 | 3 | 1 |
| α-helix | 89-90 | 2 | |
| β-strand | 95-97 | 3 | 1 |
| α-helix | 108-110 | 3 | |
| β-strand | 115-117 | 3 | 1 |
| α-helix | 128-130 | 3 | |
| β-strand | 135-137 | 3 | 1 |
| α-helix | 148-150 | 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 |
|---|---|---|---|
| β-strand | 55-62 | 8 | 2 |
| β-strand | 68-75 | 8 | 2 |
| β-strand | 80 | 1 | 3 |
| α-helix | 81-92 | 12 | |
| α-helix | 96-98 | 3 | |
| β-strand | 99-102 | 4 | 2 |
| β-strand | 107 | 1 | 2 |
| β-strand | 113 | 1 | 3 |
| α-helix | 115-117 | 3 | |
| β-strand | 124-130 | 7 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 55-62 | 8 | 5 |
| β-strand | 67-75 | 9 | 5 |
| β-strand | 80 | 1 | 6 |
| α-helix | 81-92 | 12 | |
| α-helix | 96-98 | 3 | |
| β-strand | 100-102 | 3 | 5 |
| β-strand | 107 | 1 | 5 |
| α-helix | 108-109 | 2 | |
| β-strand | 113 | 1 | 6 |
| α-helix | 115-117 | 3 | |
| β-strand | 124-129 | 6 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RING-type E3 ubiquitin transferase | A, B | protein | 240 | Shigella flexneri 5a str. M90T | A0A0H2USG1 (AlphaFold model) |
| RanBP-type and C3HC4-type zinc finger-containing protein 1 | C, D | protein | 89 | Homo sapiens | Q9BYM8 (AlphaFold model) |
>7V8E_1 RING-type E3 ubiquitin transferase (chains A, B) GPGSNEFYLKTWSEWEKNGTPGEQRNIAFNRLKICLQNQEAELNLSELDLKTLPDLPPQI TTLEIRKNLLTHLPDLPPMLKVIHAQFNQLESLPALPETLEELNAGDNKIKELPFLPENL THLRVHNNRLHILPLLPPELKLLVVSGNRLDSIPPFPDKLEGLALANNFIEQLPELPFSM NRAVLMNNNLTTLPESVLRLAQNAFVNVAGNPLSGHTMRTLQQITTGPDYSGPRIFFSMG
>7V8E_2 RanBP-type and C3HC4-type zinc finger-containing protein 1 (chains C, D) GPGSEFQDIRLWVSVEDAQMHTVTIWLTVRPDMTVASLKDMVFLDYGFPPVLQQWVIGQR LARDQETLHSHGVRQNGDSAYLYLLSARN
Mechanistic insights into the subversion of the linear ubiquitin chain assembly complex by the E3 ligase IpaH1.4 of Shigella flexneri. Liu, J., Wang, Y., Wang, D. et al. Proc Natl Acad Sci U S A (2022) 119:e2116776119-e2116776119. DOI 10.1073/pnas.2116776119 · 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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