Structure of the Legionella phosphocholine hydrolase Lem3. Determined by X-ray diffraction at 3.6 Å resolution. Released 12 Apr 2023.
Explore 8AGG in 3D Show helices and sheets RCSB PDB PDBe
8AGG contains 23 α-helices and 27 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 |
|---|---|---|---|
| β-strand | 22-24 | 3 | 1 |
| β-strand | 29-32 | 4 | 2 |
| α-helix | 35-38 | 4 | |
| α-helix | 43-50 | 8 | |
| β-strand | 51-57 | 7 | 3 |
| β-strand | 60-66 | 7 | 3 |
| β-strand | 69 | 1 | 4 |
| β-strand | 75-79 | 5 | 2 |
| β-strand | 82-90 | 9 | 1 |
| β-strand | 96-106 | 11 | 1 |
| α-helix | 114-133 | 20 | |
| α-helix | 138-145 | 8 | |
| β-strand | 166-176 | 11 | 1 |
| β-strand | 180-188 | 9 | 1 |
| β-strand | 192-196 | 5 | 3 |
| β-strand | 202-206 | 5 | 3 |
| β-strand | 208 | 1 | 5 |
| β-strand | 211-212 | 2 | 6 |
| β-strand | 218-219 | 2 | 6 |
| α-helix | 223-226 | 4 | |
| β-strand | 243 | 1 | 1 |
| β-strand | 248-252 | 5 | 3 |
| α-helix | 254-257 | 4 | |
| β-strand | 262-267 | 6 | 5 |
| β-strand | 271 | 1 | 6 |
| β-strand | 272-276 | 5 | 5 |
| α-helix | 278-283 | 6 | |
| α-helix | 286-288 | 3 | |
| α-helix | 296-326 | 31 | |
| β-strand | 337 | 1 | 7 |
| α-helix | 338-348 | 11 | |
| α-helix | 351-363 | 13 | |
| β-strand | 379 | 1 | 7 |
| α-helix | 380-388 | 9 | |
| α-helix | 390-391 | 2 | |
| β-strand | 392 | 1 | 4 |
| β-strand | 395-402 | 8 | 3 |
| α-helix | 403-405 | 3 | |
| α-helix | 406-416 | 11 | |
| α-helix | 418-420 | 3 | |
| α-helix | 425-431 | 7 | |
| α-helix | 435-446 | 12 | |
| β-strand | 449-450 | 2 | 8 |
| β-strand | 455-457 | 3 | 3 |
| β-strand | 464-465 | 2 | 8 |
| α-helix | 469-485 | 17 | |
| α-helix | 496-508 | 13 | |
| α-helix | 514-516 | 3 | |
| α-helix | 517-525 | 9 | |
| α-helix | 546-563 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Phosphocholine hydrolase Lem3 | A | protein | 572 | Legionella pneumophila | Q5ZXN5 (AlphaFold model) |
>8AGG_1 Phosphocholine hydrolase Lem3 (chains A) GHMKLRYIINENKLVFTSCNMRDKIITGKKIIFSQSVAKDQTKNLSSFLSERFYSVNQSH NHSIIIGSSLSHQENDIEHDTILDTSGVLVTTDTNGIVNGARVAITDGLGGGNGDQEEDD EIYRVSHSSCENFLNCDQNIDTTLSLITQPKASDKKQTAPKTLQHTEASMAAFIYQNHPG KGYIGEFANIGDGLIIILDKRFKIKHMVSACHIYRGFGTWTPPSLQALATTANKDALLVR QTLKLAEGDIIISMTDGVWGELKTSLIAQTNDRRDIGVDKEYFKTLFDELTDAPYPSSFD IARIITQRAMSRSLERRKTLIKLINEIEQQHFHEKSVKTINEVLEYFIKTGHVETAQTLK AILFEDGLSDGITYFENIEIPLEMVMHDLKSRTVGDCSTINVTRIPYHLDELIRGFINYP EKHQILAPLFKARVKSEADLEEAFHRLSLEMVQPEIECPISETHFERAFKKETLDKTQAV LTHYFRISTGLDSKKNYQERLNDLSAYLSKESSLEKNDIKLLLSMLDSEIKPKTGVFQTL FGENQNKLYKAFHKKIELQLLDSEIENKNELK
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
Dephosphocholination by Legionella effector Lem3 functions through remodelling of the switch II region of Rab1b. Kaspers, M.S., Pogenberg, V., Pett, C. et al. Nat Commun (2023) 14:2245-2245. DOI 10.1038/s41467-023-37621-7 · PubMed
Other PDB entries of the same protein (UniProt Q5ZXN5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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