Chlamydia pneumoniae CopN (D29 construct). Determined by X-ray diffraction at 1.77 Å resolution. Released 30 Jul 2014.
Explore 4P3Z in 3D Show helices and sheets RCSB PDB PDBe
4P3Z contains 16 α-helices and 0 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 | 96-101 | 6 | |
| α-helix | 109-118 | 10 | |
| α-helix | 125-135 | 11 | |
| α-helix | 139-152 | 14 | |
| α-helix | 158-175 | 18 | |
| α-helix | 177-184 | 8 | |
| α-helix | 186-196 | 11 | |
| α-helix | 200-211 | 12 | |
| α-helix | 217-225 | 9 | |
| α-helix | 230-250 | 21 | |
| α-helix | 257-293 | 37 | |
| α-helix | 304-316 | 13 | |
| α-helix | 322-333 | 12 | |
| α-helix | 337-353 | 17 | |
| α-helix | 356-358 | 3 | |
| α-helix | 362-382 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CopN | A | protein | 425 | Chlamydia pneumoniae | Q9Z8L4 (AlphaFold model) |
>4P3Z_1 CopN (chains A) MKHHHHHHPMSDYDIPTTENLYFQGAMAASGGTGGLGGTQGVNLAAVEAAAAKADAAEVV ASQEGSEMNMIQQSQDLTNPAAATRTKKKEEKFQTLESRKKGEAGKAEKKSESTEEKPDT DLADKYASGNSEISGQELRGLRDAIGDDASPEDILALVQEKIKDPALQSTALDYLVQTTP PSQGKLKEALIQARNTHTEQFGRTAIGAKNILFASQEYADQLNVSPSGLRSLYLEVTGDT HTCDQLLSMLQDRYTYQDMAIVSSFLMKGMATELKRQGPYVPSAQLQVLMTETRNLQAVL TSYDYFESRVPILLDSLKAEGIQTPSDLNFVKVAESYHKIINDKFPTASKVEREVRNLIG DDVDSVTGVLNLFFSALRQTSSRLFSSADKRQQLGAMIANALDAVNINNEDYPKASDFPK PYPWS
Biochemical and Structural Insights into Microtubule Perturbation by CopN from Chlamydia pneumoniae. Nawrotek, A., Guimaraes, B.G., Velours, C. et al. J Biol Chem (2014) 289:25199-25210. DOI 10.1074/jbc.M114.568436 · PubMed
Other PDB entries of the same protein (UniProt Q9Z8L4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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