Crystal structure of the Legionella pneumophila FIC domain-containing effector AnkX protein in complex with cytidine monophosphate and phosphocholine. Determined by X-ray diffraction at 2.54 Å resolution. Released 24 Apr 2013.
Explore 4BES in 3D Show helices and sheets RCSB PDB PDBe
4BES contains 33 α-helices and 9 β-strands across 1 chain. 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 | 11-16 | 6 | |
| α-helix | 19-25 | 7 | |
| α-helix | 39-44 | 6 | |
| α-helix | 48-64 | 17 | |
| α-helix | 69-70 | 2 | |
| α-helix | 74-84 | 11 | |
| α-helix | 99-100 | 2 | |
| β-strand | 106-109 | 4 | 1 |
| α-helix | 111-113 | 3 | |
| β-strand | 114 | 1 | 2 |
| α-helix | 116-124 | 9 | |
| α-helix | 126-130 | 5 | |
| β-strand | 134-137 | 4 | 1 |
| β-strand | 138-142 | 5 | 3 |
| β-strand | 144-147 | 4 | 3 |
| α-helix | 160-174 | 15 | |
| β-strand | 181-184 | 4 | 1 |
| α-helix | 190-207 | 18 | |
| α-helix | 211-227 | 17 | |
| α-helix | 235-238 | 4 | |
| α-helix | 239-243 | 5 | |
| α-helix | 245-250 | 6 | |
| α-helix | 253-256 | 4 | |
| β-strand | 266 | 1 | 2 |
| α-helix | 269-291 | 23 | |
| α-helix | 294-296 | 3 | |
| α-helix | 298-300 | 3 | |
| α-helix | 305-314 | 10 | |
| α-helix | 318-324 | 7 | |
| α-helix | 333-344 | 12 | |
| α-helix | 345-347 | 3 | |
| α-helix | 352-359 | 8 | |
| α-helix | 363-370 | 8 | |
| α-helix | 375-378 | 4 | |
| β-strand | 382 | 1 | 4 |
| β-strand | 391 | 1 | 4 |
| α-helix | 395-402 | 8 | |
| α-helix | 405-413 | 9 | |
| α-helix | 428-435 | 8 | |
| α-helix | 438-449 | 12 | |
| α-helix | 454-458 | 5 | |
| α-helix | 468-473 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Phosphocholine transferase ankx | A | protein | 484 | LEGIONELLA PNEUMOPHILA SUBSP. PNEUMOPHILA STR. PHILADELPHIA 1 | Q5ZXN6 (AlphaFold model) |
>4BES_1 PHOSPHOCHOLINE TRANSFERASE ANKX (chains A) GVKIMPNLPGLYFLQAYPSEEIWRLFVDGRFWSKENGWRGYESREPGCLNAALESLCSIA LQVEKSGEEFELSVDLIKRIHKKCGKKVEELQEKNPGELRTDEPVSFGIPAGRASIKGIE EFLSLVFLTEGGAEFGPGKAGPFGPRFDKNYFKNLNPEQIPDLAKQIYFDMCKYGHSNTN HFYLAVMKNVDVYLEKITQSYNKEIKTAETLDEKLKIIVKHIRMYEVLHPFRDANGRTFV NNLLNIPLMQQGLPPATFYEPNVFDLYSAEELVVVVKEAIFNTVEIIEQSKRKTPITLYG YHSSLEEQTKFRDMLDSPSYEKIKHMDFSDLNPEKLHLKTQKCLSSLNEQYPLHRGAIYL SDPGEIKLLLSNRNESQINQQIEQGAPPIYVGKTPAHLAVISGNMAMLDELIAKKADLSL QDYDGKTALHYAAECGNMQIMGKILKVVLSQEDAIKVLNIKDNHGKTAFHYAAEFGTPEL ISAL
Water and common crystallization additives (SO4) are not listed.
Structure of the Legionella Effector Ankx Reveals the Mechanism of Phosphocholine Transfer by the Fic Domain. Campanacci, V., Mukherjee, S., Roy, C.R. et al. EMBO J (2013) 32:1469. DOI 10.1038/EMBOJ.2013.82 · PubMed
Other PDB entries of the same protein (UniProt Q5ZXN6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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