Structure analysis

Crystal Structure of the Bromodomain of human CECR2

X-ray diffraction
1.83Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: monomeric
Accessible surface area: 6100 Å2
Buried surface area: 250 Å2
Dissociation area: 150 Å2
Dissociation energy (ΔGdiss): -2 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Interface energy (ΔGint): 3 kcal/mol
Symmetry number: 1
Assembly 2 (preferred)
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Multimeric state: monomeric
Accessible surface area: 6100 Å2
Buried surface area: 450 Å2
Dissociation area: 100 Å2
Dissociation energy (ΔGdiss): -3 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Interface energy (ΔGint): 6 kcal/mol
Symmetry number: 1

Macromolecules

Chains: A, B
Length: 116 amino acids
Theoretical weight: 13.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9BXF3 (Residues: 424-538; Coverage: 8%)
Gene names: CECR2, KIAA1740
Pfam: Bromodomain
InterPro:
CATH: Bromodomain-like

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