Crystal structure of Rab1-activation domain and P4M domain of SidM/DrrA from legionella. Determined by X-ray diffraction at 3.45 Å resolution. Released 22 Dec 2009.
Explore 3L0M in 3D Show helices and sheets RCSB PDB PDBe
3L0M contains 31 α-helices and 4 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 | 319-361 | 43 | |
| α-helix | 365-381 | 17 | |
| α-helix | 386-389 | 4 | |
| α-helix | 391-393 | 3 | |
| α-helix | 400-420 | 21 | |
| α-helix | 428-445 | 18 | |
| α-helix | 464-478 | 15 | |
| β-strand | 484-485 | 2 | 1 |
| β-strand | 488-489 | 2 | 1 |
| α-helix | 490-506 | 17 | |
| α-helix | 512-520 | 9 | |
| α-helix | 526-529 | 4 | |
| α-helix | 565-578 | 14 | |
| α-helix | 579-581 | 3 | |
| α-helix | 585-596 | 12 | |
| α-helix | 600-605 | 6 | |
| α-helix | 610-613 | 4 | |
| α-helix | 620-634 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 319-361 | 43 | |
| α-helix | 365-381 | 17 | |
| α-helix | 386-389 | 4 | |
| α-helix | 391-393 | 3 | |
| α-helix | 402-420 | 19 | |
| α-helix | 429-445 | 17 | |
| α-helix | 464-478 | 15 | |
| β-strand | 484-485 | 2 | 2 |
| β-strand | 488-489 | 2 | 2 |
| α-helix | 490-506 | 17 | |
| α-helix | 512-519 | 8 | |
| α-helix | 526-529 | 4 | |
| α-helix | 564-578 | 15 | |
| α-helix | 579-581 | 3 | |
| α-helix | 585-596 | 12 | |
| α-helix | 610-613 | 4 | |
| α-helix | 620-636 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DrrA | A, B | protein | 336 | Legionella pneumophila | Q5ZSQ3 (AlphaFold model) |
>3L0M_1 DrrA (chains A, B) GPLGSMPYSDAKAMLDEVAKIRELGVQRVTRIENLENAKKLWDNANSMLEKGNISGYLKA ANELHKFMKEKNLKEDDLRPELSDKTISPKGYAILQSLWGAASDYSRAAATLTESTVEPG LVSAVNKMSAFFMDCKLSPNERATPDPDFKVGKSKILVGIMQFIKDVADPTSKIWMHNTK ALMNHKIAAIQKLERSNNVNDETLESVLSSKGENLSEYLSYKYATKDEGREHRYTASTEN FKNVKEKYQQMRGDALKTEILADFKDKLAEATDEQSLKQIVAELKSKDEYRILAKGQGLT TQLLGLKTSSVSSFEKMVEETRESIKSQERQTIKIK
Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Zhu, Y., Hu, L., Zhou, Y. et al. Proc Natl Acad Sci U S A (2010) 107:4699-4704. DOI 10.1073/pnas.0914231107 · PubMed
Other PDB entries of the same protein (UniProt Q5ZSQ3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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