Structure analysis

Crystal structure of IRAK4 kinase domain apo form

X-ray diffraction
2Å 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: 14390.44 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-192669
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 13995.48 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-192669
Assembly 3
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Multimeric state: monomeric
Accessible surface area: 14140.36 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-192669
Assembly 4
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Multimeric state: monomeric
Accessible surface area: 14285.55 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-192669

Macromolecules

Chains: A, B, C, D
Length: 301 amino acids
Theoretical weight: 33.96 KDa
Source organism: Homo sapiens
Expression system: unidentified baculovirus
UniProt:
  • Canonical: Q9NWZ3 (Residues: 160-460; Coverage: 65%)
Gene name: IRAK4
Pfam: Protein tyrosine and serine/threonine kinase
InterPro:
CATH:

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