Structure analysis

Crystal structure of human ATAD2 bromodomain in complex with 5-5- methoxypyridin-3-yl-3-methyl-8-piperidin-4-ylamino-1,2-dihydro-1,7- naphthyridin-2-one

X-ray diffraction
2.01Å 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: 15826.91 Å2
Buried surface area: 2292.76 Å2
Dissociation area: 404.42 Å2
Dissociation energy (ΔGdiss): 13.58 kcal/mol
Dissociation entropy (TΔSdiss): 14.24 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-180200

Macromolecules

Chain: A
Length: 130 amino acids
Theoretical weight: 15.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6PL18 (Residues: 981-1108; Coverage: 9%)
Gene names: ATAD2, L16, PRO2000
Pfam: Bromodomain
InterPro:
CATH: Bromodomain-like
PDBe-KB: UniProt Coverage View: Q6PL18  
1130102030405060708090100110120130
 
50100
UniProt
Q6PL18
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces
Sequence conservation

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