Structure analysis

Crystal Structure Of The Human P21-Activated Kinase 5

X-ray diffraction
1.8Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: monomeric
Accessible surface area: 14746.75 Å2
Buried surface area: 343.64 Å2
Dissociation area: 150.03 Å2
Dissociation energy (ΔGdiss): -5.57 kcal/mol
Dissociation entropy (TΔSdiss): 3.72 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-192827
Assembly 2 (preferred)
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Multimeric state: monomeric
Accessible surface area: 14882.86 Å2
Buried surface area: 734.97 Å2
Dissociation area: 367.48 Å2
Dissociation energy (ΔGdiss): 0.47 kcal/mol
Dissociation entropy (TΔSdiss): 4.66 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-192827

Macromolecules

Chains: A, B
Length: 317 amino acids
Theoretical weight: 36.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9P286 (Residues: 425-719; Coverage: 41%)
Gene names: KIAA1264, PAK5, PAK7
Pfam: Protein kinase domain
InterPro:
CATH:

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