9HGH: MyD88 peptide_1

MyD88 peptide_1 bound to SPOP MATH domain. Determined by X-ray diffraction at 1.9 Å resolution. Released 23 Apr 2025.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Homo sapiens
Chains
2
Atoms
1,340
Mol. weight
17.98 kDa
Released
23 Apr 2025

Explore 9HGH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9HGH contains 6 α-helices and 11 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: 6 helices, 10 β-strands

ElementResiduesLengthSheet
β-strand29-38101
α-helix41-433
β-strand52-5322
α-helix54-563
β-strand5712
β-strand66-7272
α-helix78-803
β-strand83-92102
β-strand98-107101
β-strand113-11861
β-strand123-12531
β-strand130-13892
α-helix139-1435
α-helix145-1473
α-helix151-1533
β-strand155-164101
Chain B: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand13512

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Speckle type BTB/POZ proteinAprotein140Homo sapiensD6RDG8 (AlphaFold model)
Myeloid differentiation primary response protein MyD88Bprotein17Homo sapiensQ99836 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9HGH_1 Speckle type BTB/POZ protein (chains A)
AKVVKFSYMWTINNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSL
YLLLVSCPKSEVRAKFKFSILNAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEA
NGLLPDDKLTLFCEVSVVQD
Sequence of entity 2 (B), FASTA
>9HGH_2 Myeloid differentiation primary response protein MyD88 (chains B)
AEKPLQVAAVDSSVPRT

Primary citation

Sequence rules for a long SPOP-binding degron required for protein ubiquitylation. Makhlouf, L., Mishra, M., Makhlouf, H. et al. Biochem J (2025) 482:583-600. DOI 10.1042/BCJ20253041 · PubMed

Other PDB entries of the same protein (UniProt D6RDG8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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