structure of the phosphothreonine lyase SpvC, the effector protein from Salmonella. Determined by X-ray diffraction at 2.3 Å resolution. Released 11 Dec 2007.
Explore 2P1W in 3D Show helices and sheets RCSB PDB PDBe
2P1W contains 12 α-helices and 10 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 | 29-35 | 7 | |
| α-helix | 37-44 | 8 | |
| α-helix | 48-50 | 3 | |
| α-helix | 61-64 | 4 | |
| β-strand | 70-73 | 4 | 1 |
| β-strand | 76-79 | 4 | 1 |
| β-strand | 86-91 | 6 | 1 |
| β-strand | 103-107 | 5 | 1 |
| β-strand | 109 | 1 | 2 |
| α-helix | 111-113 | 3 | |
| α-helix | 114-125 | 12 | |
| β-strand | 134-138 | 5 | 1 |
| α-helix | 140-145 | 6 | |
| β-strand | 155-158 | 4 | 1 |
| α-helix | 167-169 | 3 | |
| α-helix | 170-189 | 20 | |
| α-helix | 192-193 | 2 | |
| β-strand | 194 | 1 | 2 |
| β-strand | 202 | 1 | 1 |
| β-strand | 210-214 | 5 | 1 |
| α-helix | 227-230 | 4 | |
| α-helix | 234-240 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 27.5 kDa virulence protein | A | protein | 250 | Salmonella enteritidis | P0A2N1 (AlphaFold model) |
>2P1W_1 27.5 kDa virulence protein (chains A) GPLGSPGRPMPINRPNLNLNIPPLNIVAAYDGAEIPSTNKHLKNNFNSLHNQMRKMPVSH FKEALDVPDYSGMRQSGFFAMSQGFQLNNHGYDVFIHARRESPQSQGKFAGDKFHISVLR DMVPQAFQALSGLLFSEDSPVDKWKVTDMEKVVQQARVSLGAQFTLYIKPDQENSQYSAS FLHKTRQFIECLESRLSENGVISGQCPESDVHPENWKYLSYRNELRSGRDGGEMQRQALR EEPFYRLMTE
Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase. Zhu, Y., Li, H., Long, C. et al. Mol Cell (2007) 28:899-913. DOI 10.1016/j.molcel.2007.11.011 · PubMed
Other PDB entries of the same protein (UniProt P0A2N1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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