Structure analysis

Crystal structure of human TDRD1 extended Tudor domain in complex with a symmetrically dimethylated E2F peptide

X-ray diffraction
1.95Å resolution
Source organism: Homo sapiens
Assemblies composition:
hetero dimer (preferred)
monomeric
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 11504.93 Å2
Buried surface area: 1017.11 Å2
Dissociation area: 280.24 Å2
Dissociation energy (ΔGdiss): -1.24 kcal/mol
Dissociation entropy (TΔSdiss): 5.48 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-169518
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 11085.07 Å2
Buried surface area: 212.2 Å2
Dissociation area: 106.1 Å2
Dissociation energy (ΔGdiss): -0.93 kcal/mol
Dissociation entropy (TΔSdiss): -0.28 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-189801

Macromolecules

Chains: A, B
Length: 220 amino acids
Theoretical weight: 24.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BXT4 (Residues: 460-679; Coverage: 19%)
Gene name: TDRD1
Pfam: Tudor domain
InterPro:

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Chain: C
Length: 17 amino acids
Theoretical weight: 1.76 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q01094 (Residues: 104-120; Coverage: 4%)
Gene names: E2F1, RBBP3

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