Structure analysis

Symmetric Dimethylation of H3 Arginine 2 is a Novel Histone Mark that Supports Euchromatin Maintenance

X-ray diffraction
1.9Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 11881.27 Å2
Buried surface area: 1123.66 Å2
Dissociation area: 561.83 Å2
Dissociation energy (ΔGdiss): 4.33 kcal/mol
Dissociation entropy (TΔSdiss): 6.36 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-158475

Macromolecules

Chain: A
Length: 318 amino acids
Theoretical weight: 34.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P61964 (Residues: 21-334; Coverage: 94%)
Gene names: BIG3, WDR5
Pfam: WD domain, G-beta repeat
InterPro:
CATH: YVTN repeat-like/Quinoprotein amine dehydrogenase

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Chain: B
Length: 16 amino acids
Theoretical weight: 1.72 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P68431 (Residues: 1-16; Coverage: 12%)
Gene names: H3C1, H3C10, H3C11, H3C12, H3C2, H3C3, H3C4, H3C6, H3C7, H3C8, H3FA, H3FB, H3FC HIST1H3C, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL, HIST1H3A, HIST1H3B, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J

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