Structure analysis

Crystal structure of Human histone acetytransferas 1 (HAT1) in complex with isobutryl-COA and K12A mutant variant of histone H4

X-ray diffraction
1.6Å 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: 16813.06 Å2
Buried surface area: 3208.55 Å2
Dissociation area: 738.01 Å2
Dissociation energy (ΔGdiss): 2.92 kcal/mol
Dissociation entropy (TΔSdiss): 8.31 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-127202
Assembly 2
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Multimeric state: hetero dimer
Accessible surface area: 16628.78 Å2
Buried surface area: 3323.97 Å2
Dissociation area: 720.06 Å2
Dissociation energy (ΔGdiss): 1.9 kcal/mol
Dissociation entropy (TΔSdiss): 8.07 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-127202

Macromolecules

Chains: A, B
Length: 324 amino acids
Theoretical weight: 38.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O14929 (Residues: 20-341; Coverage: 77%)
  • Best match: O14929-2 (Residues: 1-256)
Gene names: HAT1, KAT1
Pfam:
InterPro:

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Chains: C, D
Length: 20 amino acids
Theoretical weight: 1.94 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P62805 (Residues: 2-21; Coverage: 19%)
Gene names: H4-16, H4/A, H4/B, H4/C, H4/D, H4/E, H4/G, H4/H, H4/I, H4/J, H4/K, H4/M, H4/N, H4/O, H4C1, H4C11, H4C12, H4C13, H4C14, H4C15, H4C16, H4C2, H4C3, H4C4, H4C5, H4C6, H4C8, H4C9, H4F2, H4FA, H4FB, H4FC, H4FD, H4FE, H4FG, H4FH, H4FI, H4FJ, H4FK, H4FM, H4FN, H4FO, HIST1H4A, HIST1H4B, HIST1H4C, HIST1H4D, HIST1H4E, HIST1H4F, HIST1H4H, HIST1H4I, HIST1H4J, HIST1H4K, HIST1H4L, HIST2H4, HIST2H4A, HIST2H4B, HIST4H4
InterPro: Histone H4, conserved site

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