MavC-Lpg2149 complex. Determined by X-ray diffraction at 2.7 Å resolution. Released 20 May 2020.
Explore 7BXH in 3D Show helices and sheets RCSB PDB PDBe
7BXH contains 29 α-helices and 12 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 | 12-36 | 25 | |
| α-helix | 44-53 | 10 | |
| α-helix | 70-77 | 8 | |
| α-helix | 79-82 | 4 | |
| α-helix | 92-109 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-24 | 15 | |
| α-helix | 25-29 | 5 | |
| α-helix | 33-42 | 10 | |
| α-helix | 45-47 | 3 | |
| α-helix | 54-63 | 10 | |
| α-helix | 70-71 | 2 | |
| α-helix | 74-96 | 23 | |
| β-strand | 100-101 | 2 | 1 |
| α-helix | 102-103 | 2 | |
| α-helix | 107-110 | 4 | |
| β-strand | 118-126 | 9 | 1 |
| β-strand | 132-135 | 4 | 2 |
| α-helix | 138-140 | 3 | |
| α-helix | 147 | 1 | |
| β-strand | 150-153 | 4 | 2 |
| β-strand | 158-161 | 4 | 2 |
| β-strand | 167-169 | 3 | 2 |
| α-helix | 174-183 | 10 | |
| α-helix | 187-190 | 4 | |
| β-strand | 191-193 | 3 | 2 |
| α-helix | 201-203 | 3 | |
| α-helix | 205-220 | 16 | |
| α-helix | 221-223 | 3 | |
| β-strand | 228-237 | 10 | 1 |
| β-strand | 249-251 | 3 | 1 |
| β-strand | 254 | 1 | 3 |
| β-strand | 258 | 1 | 3 |
| α-helix | 260-265 | 6 | |
| α-helix | 268-273 | 6 | |
| α-helix | 277-289 | 13 | |
| α-helix | 293-304 | 12 | |
| α-helix | 306 | 1 | |
| α-helix | 316-318 | 3 | |
| β-strand | 324-332 | 9 | 1 |
| α-helix | 335-352 | 18 | |
| α-helix | 358-380 | 23 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lpg2149 | A | protein | 105 | Legionella pneumophila subsp. pneumophila str. Philadelphia 1 | Q5ZTL2 (AlphaFold model) |
| MavC | B | protein | 386 | Legionella pneumophila subsp. pneumophila str. Philadelphia 1 | Q5ZTL4 (AlphaFold model) |
>7BXH_1 Lpg2149 (chains A) SGTFFKDYQKKNVMRLLQDSLEKIINEWLKTDDESHTKLKSLQELSEMDINATSFAEHSP LPDFVTRLWLDPHKALDAMDKNISKNEIRKLIKETAREIELVFTH
>7BXH_2 MavC (chains B) SMTTSKLEKTGLHVHEKIKHMVKNYGTMITGIPAEILGQNEAEISVGYVKKMGNMKENIA EVVRKSEMTQPTNSCGKASNEVCDLLLGTEGASEFEKSSYQVLSGDGSNLKGSLPNKNLL VRVEMDRFNAPQKYQKIKREEFNPETAEKNKIYLLEDQLVYLDIFGKVIDLGQTSDTCHR LFNAITTPFYQNYILYDEYIDPEESAEEAAMFEMGEIVKAKMKNIDCWTATHSFTIFVPE SDSEDTRTLYPYQAYWTSHTLQQWFSGDKDEKLSRLGIDGYIEKLALLGTTTDSKIRSSI YGELFSPPGKEHVFCTGMNEKFSPLRVKFKVTEVNPEIALQNLEEVQEFIDTNYPGENAK DQCELYKIKAQEAMTKQLEMRLLIEP
Insights into catalysis and regulation of non-canonical ubiquitination and deubiquitination by bacterial deamidase effectors. Wang, Y., Zhan, Q., Wang, X. et al. Nat Commun (2020) 11:2751-2751. DOI 10.1038/s41467-020-16587-w · PubMed
Other PDB entries of the same protein (UniProt Q5ZTL2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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