8J2P: PML B-box2

Crystal structure of PML B-box2. Determined by X-ray diffraction at 2.09 Å resolution. Released 20 Sept 2023.

Method
X-ray diffraction
Resolution
2.09 Å
Organisms
Escherichia coli (strain K12), Homo sapiens
Chains
2
Atoms
6,736
Mol. weight
94.99 kDa
Ligands
ZN
Released
20 Sept 2023

Explore 8J2P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8J2P contains 50 α-helices and 54 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.

Chain A: 25 helices, 27 β-strands

ElementResiduesLengthSheet
β-strand-183--180410
α-helix-173--15915
β-strand-155--152410
α-helix-147--1399
β-strand-131--127510
α-helix-126--1243
α-helix-123--1186
β-strand-114111
α-helix-113--1113
α-helix-107--1044
β-strand-101112
α-helix-99--946
β-strand-92--91213
β-strand-88--87213
β-strand-84--79610
β-strand-76--72514
β-strand-62115
α-helix-61--593
α-helix-58--509
β-strand-45--43314
α-helix-36--2710
β-strand-23--19516
β-strand-15--8816
α-helix-4-1015
α-helix20-289
β-strand32-37614
α-helix39-413
α-helix42-465
β-strand52-55414
α-helix56-583
β-strand59-60215
β-strand63-64215
α-helix671
β-strand68-69217
β-strand70-76710
β-strand77111
α-helix83-897
α-helix90-945
α-helix97-10610
β-strand111-112210
β-strand114112
α-helix115-1217
α-helix125-13612
β-strand138-139217
α-helix140-1412
α-helix146-16116
α-helix167-18115
β-strand187-188218
β-strand199-200218
β-strand202-204316
β-strand210-211216
α-helix213-2186
Chain E: 25 helices, 27 β-strands
ElementResiduesLengthSheet
β-strand-184--18051
α-helix-173--15915
β-strand-156--15251
α-helix-147--1399
β-strand-131--12751
α-helix-126--1243
α-helix-123--1186
β-strand-11412
α-helix-113--1113
α-helix-107--1044
β-strand-10113
α-helix-99--946
β-strand-92--9124
β-strand-88--8724
β-strand-84--7961
β-strand-76--7255
β-strand-6216
α-helix-61--593
α-helix-58--509
β-strand-45--4335
α-helix-36--2710
β-strand-23--1867
β-strand-15--887
α-helix-4-1015
α-helix20-289
β-strand32-3765
α-helix39-413
α-helix42-465
β-strand52-5545
α-helix56-583
β-strand59-6026
β-strand63-6426
α-helix671
β-strand68-6928
β-strand70-7671
β-strand7712
α-helix83-897
α-helix90-945
α-helix97-10610
β-strand111-11221
β-strand11413
α-helix115-1217
α-helix125-13612
β-strand138-13928
α-helix140-1412
α-helix146-16116
α-helix167-18115
β-strand187-18829
β-strand199-20029
β-strand202-20437
β-strand210-21127
α-helix213-2186

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Maltose/maltodextrin-binding periplasmic protein,Protein PMLA, Eprotein428Escherichia coli (strain K12), Homo sapiensP0AEX9 (AlphaFold model), P29590 (AlphaFold model)
Sequence of entity 1 (A, E), FASTA
>8J2P_1 Maltose/maltodextrin-binding periplasmic protein,Protein PML (chains A, E)
MGKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPD
IIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYN
KDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDI
KDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS
KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKP
LGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD
EALKDAQTNAAAEFKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCD
ISAEIQQR

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn4

Primary citation

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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