Crystal structure of MvcA from Legionella pneumophila. Determined by X-ray diffraction at 1.94 Å resolution. Released 18 Dec 2019.
Explore 6K11 in 3D Show helices and sheets RCSB PDB PDBe
6K11 contains 50 α-helices and 24 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 | 16-31 | 16 | |
| α-helix | 32-36 | 5 | |
| α-helix | 40-51 | 12 | |
| α-helix | 52-54 | 3 | |
| α-helix | 61-76 | 16 | |
| α-helix | 83-95 | 13 | |
| α-helix | 97-105 | 9 | |
| α-helix | 107-108 | 2 | |
| β-strand | 109-110 | 2 | 1 |
| α-helix | 111-112 | 2 | |
| α-helix | 116-123 | 8 | |
| β-strand | 132-141 | 10 | 1 |
| β-strand | 146-149 | 4 | 2 |
| α-helix | 152-154 | 3 | |
| α-helix | 161 | 1 | |
| β-strand | 164-167 | 4 | 2 |
| β-strand | 172-175 | 4 | 2 |
| β-strand | 181-183 | 3 | 2 |
| α-helix | 188-197 | 10 | |
| β-strand | 204-205 | 2 | 2 |
| α-helix | 209-213 | 5 | |
| α-helix | 218-232 | 15 | |
| α-helix | 234-236 | 3 | |
| β-strand | 240-250 | 11 | 1 |
| α-helix | 251-254 | 4 | |
| α-helix | 257-259 | 3 | |
| β-strand | 262-264 | 3 | 1 |
| β-strand | 267 | 1 | 3 |
| β-strand | 271 | 1 | 3 |
| α-helix | 273-278 | 6 | |
| α-helix | 281-286 | 6 | |
| α-helix | 290-300 | 11 | |
| α-helix | 306-317 | 12 | |
| α-helix | 319 | 1 | |
| α-helix | 329-331 | 3 | |
| β-strand | 337-345 | 9 | 1 |
| α-helix | 348-363 | 16 | |
| α-helix | 370-393 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 16-31 | 16 | |
| α-helix | 32-36 | 5 | |
| α-helix | 40-51 | 12 | |
| α-helix | 52-54 | 3 | |
| α-helix | 61-75 | 15 | |
| α-helix | 83-105 | 23 | |
| α-helix | 107-108 | 2 | |
| β-strand | 109-110 | 2 | 4 |
| α-helix | 111-112 | 2 | |
| α-helix | 116-123 | 8 | |
| β-strand | 132-141 | 10 | 4 |
| β-strand | 146-149 | 4 | 5 |
| α-helix | 152-154 | 3 | |
| α-helix | 161 | 1 | |
| β-strand | 164-167 | 4 | 5 |
| β-strand | 172-175 | 4 | 5 |
| β-strand | 181-183 | 3 | 5 |
| α-helix | 188-197 | 10 | |
| β-strand | 203-205 | 3 | 5 |
| α-helix | 218-232 | 15 | |
| α-helix | 234-236 | 3 | |
| β-strand | 240-250 | 11 | 4 |
| α-helix | 251-253 | 3 | |
| α-helix | 257-259 | 3 | |
| β-strand | 262-264 | 3 | 4 |
| β-strand | 267 | 1 | 6 |
| β-strand | 271 | 1 | 6 |
| α-helix | 273-279 | 7 | |
| α-helix | 281-286 | 6 | |
| α-helix | 290-302 | 13 | |
| α-helix | 306-317 | 12 | |
| α-helix | 319 | 1 | |
| α-helix | 329-331 | 3 | |
| β-strand | 337-345 | 9 | 4 |
| α-helix | 348-363 | 16 | |
| α-helix | 370-393 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lpg2148(MvcA) | A, B | protein | 383 | Legionella pneumophila subsp. pneumophila str. Philadelphia 1 | Q5ZTL3 (AlphaFold model) |
>6K11_1 Lpg2148(MvcA) (chains A, B) LESPGFMVHKKLKSMSQSYGVMMTGVPAEVLGQMQAERSIPSINKTGNLKQQIAKEVSKV CHMMTEPTQSCGQASNDVCELLLGKIEAEKFHFTKYEALSADGDNLKNVLENTAPSSTNL LIRFEIDREDPPIVLVKTKNENFNPETAVKNKIYLLENKLYFIDKMGNLFNLGPGKKKCT QLFNAIGDSAEYSLCDPFVLEEPEKPEDFAISEIVDIFNEQKERFDFWIGSHSFTIYIPQ TLGESPRQFYPYQAYFGSHTLQDWFVSDKDEYLSRIGIDKYIEKLAVLGKTTNTKERSDI YAEFFSKRGREAFFCAHLNEKRQPLRVKFKITEINPELALKNLQETQEFIDTHPGENPSD KVENYRNRAKLAMTEHLESLLDI
Legionella pneumophila regulates the activity of UBE2N by deamidase-mediated deubiquitination. Gan, N., Guan, H., Huang, Y. et al. EMBO J (2020) 39:e102806-e102806. DOI 10.15252/embj.2019102806 · PubMed
Other PDB entries of the same protein (UniProt Q5ZTL3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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