Structure analysis

Crystal structure of histone lysine methyltransferase g9a with an inhibitor

X-ray diffraction
2.56Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 24233.08 Å2
Buried surface area: 2551.06 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-188603

Macromolecules

Chains: A, B
Length: 283 amino acids
Theoretical weight: 32.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q96KQ7 (Residues: 913-1193; Coverage: 23%)
Gene names: BAT8, C6orf30, EHMT2, G9A, KMT1C, NG36
Pfam:
InterPro:
CATH: SET domain

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