Crystal structure of PML B-box2 mutant. Determined by X-ray diffraction at 2.6 Å resolution. Released 20 Sept 2023.
Explore 8J25 in 3D Show helices and sheets RCSB PDB PDBe
8J25 contains 25 α-helices and 28 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 | -183--180 | 4 | 1 |
| α-helix | -173--159 | 15 | |
| β-strand | -155--152 | 4 | 1 |
| α-helix | -147--140 | 8 | |
| α-helix | -139--137 | 3 | |
| β-strand | -131--127 | 5 | 1 |
| α-helix | -126--124 | 3 | |
| α-helix | -123--118 | 6 | |
| β-strand | -114 | 1 | 2 |
| α-helix | -107--104 | 4 | |
| β-strand | -101 | 1 | 3 |
| α-helix | -99--94 | 6 | |
| β-strand | -92--91 | 2 | 4 |
| β-strand | -88--87 | 2 | 4 |
| β-strand | -84--79 | 6 | 1 |
| β-strand | -76--72 | 5 | 5 |
| β-strand | -62 | 1 | 6 |
| α-helix | -58--50 | 9 | |
| β-strand | -45--43 | 3 | 5 |
| α-helix | -36--27 | 10 | |
| β-strand | -23--19 | 5 | 7 |
| β-strand | -15--8 | 8 | 7 |
| α-helix | -4-10 | 15 | |
| α-helix | 20-28 | 9 | |
| β-strand | 32-37 | 6 | 5 |
| α-helix | 39-41 | 3 | |
| α-helix | 42-47 | 6 | |
| β-strand | 52-55 | 4 | 5 |
| α-helix | 56-58 | 3 | |
| β-strand | 59 | 1 | 6 |
| β-strand | 60 | 1 | 8 |
| β-strand | 63 | 1 | 8 |
| α-helix | 64-65 | 2 | |
| α-helix | 67 | 1 | |
| β-strand | 68-69 | 2 | 9 |
| β-strand | 70-76 | 7 | 1 |
| β-strand | 77 | 1 | 2 |
| α-helix | 83-89 | 7 | |
| α-helix | 90-94 | 5 | |
| α-helix | 97-104 | 8 | |
| β-strand | 111-112 | 2 | 1 |
| β-strand | 114 | 1 | 3 |
| α-helix | 115-121 | 7 | |
| α-helix | 125-136 | 12 | |
| β-strand | 138-139 | 2 | 9 |
| α-helix | 140-141 | 2 | |
| α-helix | 146-162 | 17 | |
| α-helix | 167-181 | 15 | |
| β-strand | 187-188 | 2 | 10 |
| β-strand | 199-200 | 2 | 10 |
| β-strand | 202-204 | 3 | 7 |
| β-strand | 209-210 | 2 | 7 |
| α-helix | 213-218 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose/maltodextrin-binding periplasmic protein,Protein PML | A | protein | 428 | Escherichia coli (strain K12), Homo sapiens | P0AEX9 (AlphaFold model), P29590 (AlphaFold model) |
>8J25_1 Maltose/maltodextrin-binding periplasmic protein,Protein PML (chains A) MGKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPD IIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYN KDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDI KDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKP LGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD EALKDAQTNAAAEFKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCASCVLLDSSHSELKCD ISAEIQQR
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Structural Basis of PML-RARA Oncoprotein Targeting by Arsenic Unravels a Cysteine Rheostat Controlling PML Body Assembly and Function. Bercier, P., Wang, Q.Q., Zang, N. et al. Cancer Discov (2023) 13:2548-2565. DOI 10.1158/2159-8290.CD-23-0453 · PubMed
Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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