Chlamydia pneumoniae CopN. Determined by X-ray diffraction at 1.2 Å resolution. Released 30 Jul 2014.
Explore 4P40 in 3D Show helices and sheets RCSB PDB PDBe
4P40 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 | 97-101 | 5 | |
| α-helix | 109-118 | 10 | |
| α-helix | 125-135 | 11 | |
| α-helix | 139-152 | 14 | |
| α-helix | 155-157 | 3 | |
| 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 | 362-382 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CopN | A | protein | 425 | Chlamydia pneumoniae | Q9Z8L4 (AlphaFold model) |
>4P40_1 CopN (chains A) MKHHHHHHPMSDYDIPTTENLYFQGAMAASGGTGGLGGTQGVNLAAVEAAAAKADAAEVV ASQEGSEMNMIQQSQDLTNPAAATRTKKKEEKFQTLESRKKGEAGKAEKKSESTEEKPDT DLADKYASGNSEISGQELRGLRDAIGDDASPEDILALVQEKIKDPALQSTALDYLVQTTP PSQGKLKEALIQARNTHTEQFGRTAIGAKNILFASQEYADQLNVSPSGLRSLYLEVTGDT HTCDQLLSMLQDRYTYQDMAIVSSFLMKGMATELKRQGPYVPSAQLQVLMTETRNLQAVL TSYDYFESRVPILLDSLKAEGIQTPSDLNFVKVAESYHKIINDKFPTASKVEREVRNLIG DDVDSVTGVLNLFFSALRQTSSRLFSSADKRQQLGAMIANALDAVNINNEDYPKASDFPK PYPWS
Water and common crystallization additives (CL, SO4) are not listed.
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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