Structure analysis

Crystal structure of selenomethionine-derived human BFK

X-ray diffraction
2.45Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 7315.68 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-178320
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 7960.53 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-178320
Assembly 3
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Multimeric state: monomeric
Accessible surface area: 8039.79 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-178320

Macromolecules

Chains: A, B, C
Length: 183 amino acids
Theoretical weight: 20.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5TBC7 (Residues: 1-163; Coverage: 100%)
Gene names: BCL2L15, C1orf178
InterPro: Bcl-2-like protein 15

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