Crystal structure of the Legionella pneumophila LegK7 effector kinase. Determined by X-ray diffraction at 2.65 Å resolution. Released 30 Dec 2020.
Explore 7BYK in 3D Show helices and sheets RCSB PDB PDBe
7BYK contains 64 α-helices and 28 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 | 1-7 | 7 | |
| α-helix | 14-22 | 9 | |
| α-helix | 28-43 | 16 | |
| α-helix | 49-55 | 7 | |
| α-helix | 63-68 | 6 | |
| β-strand | 76 | 1 | 1 |
| α-helix | 78-91 | 14 | |
| α-helix | 106-119 | 14 | |
| α-helix | 122-124 | 3 | |
| α-helix | 126-142 | 17 | |
| α-helix | 144-168 | 25 | |
| α-helix | 172-174 | 3 | |
| α-helix | 176-177 | 2 | |
| β-strand | 194-197 | 4 | 1 |
| α-helix | 205 | 1 | |
| β-strand | 206-210 | 5 | 1 |
| α-helix | 217-222 | 6 | |
| α-helix | 226-230 | 5 | |
| α-helix | 232-233 | 2 | |
| β-strand | 234-243 | 10 | 1 |
| β-strand | 249-258 | 10 | 1 |
| α-helix | 263 | 1 | |
| β-strand | 264 | 1 | 2 |
| α-helix | 265-273 | 9 | |
| α-helix | 277-279 | 3 | |
| α-helix | 280-300 | 21 | |
| β-strand | 304 | 1 | 3 |
| α-helix | 310-312 | 3 | |
| β-strand | 313-315 | 3 | 2 |
| β-strand | 320-322 | 3 | 2 |
| β-strand | 329 | 1 | 3 |
| β-strand | 335 | 1 | 4 |
| α-helix | 336-338 | 3 | |
| α-helix | 343-345 | 3 | |
| α-helix | 348-351 | 4 | |
| β-strand | 354-356 | 3 | 5 |
| β-strand | 362-365 | 4 | 5 |
| α-helix | 367-370 | 4 | |
| β-strand | 373 | 1 | 4 |
| α-helix | 376-394 | 19 | |
| α-helix | 412-414 | 3 | |
| α-helix | 420-432 | 13 | |
| α-helix | 437-439 | 3 | |
| α-helix | 441-442 | 2 | |
| α-helix | 443-450 | 8 | |
| α-helix | 457-467 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1-7 | 7 | |
| α-helix | 14-22 | 9 | |
| α-helix | 28-43 | 16 | |
| α-helix | 49-55 | 7 | |
| α-helix | 63-69 | 7 | |
| β-strand | 76 | 1 | 6 |
| α-helix | 78-91 | 14 | |
| α-helix | 106-119 | 14 | |
| α-helix | 122-125 | 4 | |
| α-helix | 126-142 | 17 | |
| α-helix | 144-168 | 25 | |
| α-helix | 172-174 | 3 | |
| α-helix | 176-177 | 2 | |
| β-strand | 194-197 | 4 | 6 |
| α-helix | 205 | 1 | |
| β-strand | 206-210 | 5 | 6 |
| α-helix | 217-222 | 6 | |
| α-helix | 226-230 | 5 | |
| α-helix | 232-233 | 2 | |
| β-strand | 234-243 | 10 | 6 |
| β-strand | 249-258 | 10 | 6 |
| α-helix | 263 | 1 | |
| β-strand | 264 | 1 | 7 |
| α-helix | 265-273 | 9 | |
| α-helix | 277-279 | 3 | |
| α-helix | 280-300 | 21 | |
| β-strand | 304 | 1 | 8 |
| α-helix | 310-312 | 3 | |
| β-strand | 313-316 | 4 | 7 |
| β-strand | 319-322 | 4 | 7 |
| β-strand | 329 | 1 | 8 |
| β-strand | 335 | 1 | 9 |
| α-helix | 336-338 | 3 | |
| α-helix | 343-345 | 3 | |
| α-helix | 348-351 | 4 | |
| β-strand | 354-356 | 3 | 10 |
| β-strand | 362-365 | 4 | 10 |
| α-helix | 367-370 | 4 | |
| β-strand | 373 | 1 | 9 |
| α-helix | 376-394 | 19 | |
| α-helix | 412-414 | 3 | |
| α-helix | 420-432 | 13 | |
| α-helix | 437-439 | 3 | |
| α-helix | 441-442 | 2 | |
| α-helix | 443-450 | 8 | |
| α-helix | 457-467 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| LegK7 | A, B | protein | 477 | Legionella pneumophila | Q5ZU83 (AlphaFold model) |
>7BYK_1 LegK7 (chains A, B) GSAKDPMPLNLPPKSSKNTMPLVIAYNNAPEDDKIQKLFYLQKINYLLNKTQLNDDLFDW INDAEEGGWLNELAKFSINPNASFFLKGMQFAKAITEEIKNKPEINSSEVNIYHLMQERD QLLKEVEFEKCATRYAEINFLLNELALNDKKTKEIVERQTEILRLVAPKIKAIKGESIDN LPVIPSYKTKELGNHVNNFNFKFTMSGWEAPFVFRVEDRHELGKEQELHSYGVSKYFIED YSVFMMRFKAEDGSTVYKPVILSQFANQNNLEEIAKQLKDGSPKNIAPRIGYYFVQLTDF CLKLIETHNYHPDIKLNNFLVHNNRVLVSDRKTFTTNDNPLASEILTSPLFAPDEFLKCL LFNKEGDPVGYNRNALWKRMNMPQFMAYQLGMALKQFLILTQLDELPDDFRNPDHSAVSH FKTPSRQIINLSLLVQELTRLDPDKRMTIKQFQTLLNFKNLPPDAFYQKVEEVFPSS
Activation of the Legionella pneumophila LegK7 Effector Kinase by the Host MOB1 Protein. Park, S.C., Cho, S.Y., Kim, T.H. et al. J Mol Biol (2020) 433:166746-166746. DOI 10.1016/j.jmb.2020.166746 · PubMed
Other PDB entries of the same protein (UniProt Q5ZU83 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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