8HDG: Uncharacterized protein DKFZp686B01123

Small peptide enhances the binding of nutline-3a to MdmX. Determined by X-ray diffraction at 1.73 Å resolution. Released 30 Nov 2022.

Method
X-ray diffraction
Resolution
1.73 Å
Organism
Homo sapiens
Chains
4
Atoms
3,483
Mol. weight
54.32 kDa
Ligands
O4B, NUT
Released
30 Nov 2022

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

Secondary structure: helices and β-sheets

8HDG contains 20 α-helices and 26 β-strands across 4 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.

Chains A and B: 5 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix13-197
β-strand26-2723
β-strand28-2924
α-helix31-399
β-strand47-4823
α-helix49-6214
β-strand6615
β-strand73-7535
α-helix80-856
β-strand89-9135
α-helix96-10510
β-strand106-10724
Chains C and D: 5 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix13-197
β-strand26-2946
α-helix31-399
β-strand47-4826
α-helix49-6214
β-strand6617
β-strand73-7537
α-helix80-856
β-strand89-9137
α-helix96-10510
β-strand106-10836

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Uncharacterized protein DKFZp686B01123A, B, C, Dprotein111Homo sapiensO15151 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>8HDG_1 Uncharacterized protein DKFZp686B01123 (chains A, B, C, D)
MGSSHHHHHHSQDLENLYFQGSQINQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYI
MVKQLYDQQEQHMVYCGGDLLGELLGRQSFSVKDPSPLYDMLRKNLVTLAT

Ligands and cofactors

IDNameFormulaCopies
O4B1,4,7,10,13,16-hexaoxacyclooctadecaneC12 H24 O64
NUT4-({(4S,5R)-4,5-bis(4-chlorophenyl)-2-[4-methoxy-2-(propan-2-yloxy)phenyl]-4,5-…C30 H30 Cl2 N4 O44

Primary citation

Small peptide enhances the binding of nutline-3a to MdmX. Cheng, X.Y., Huang, Y., Wei, Q.Y. et al. To be published.

Other PDB entries of the same protein (UniProt O15151 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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