Structure analysis

Catalytic domain of human ZIP kinase phosphorylated at Thr265

X-ray diffraction
3.1Å 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: 24210.75 Å2
Buried surface area: 3733.9 Å2
Dissociation area: 1,744.86 Å2
Dissociation energy (ΔGdiss): 3.49 kcal/mol
Dissociation entropy (TΔSdiss): 13.66 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-128886

Macromolecules

Chains: A, B
Length: 278 amino acids
Theoretical weight: 32.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43293 (Residues: 1-277; Coverage: 61%)
Gene names: DAPK3, ZIPK
Pfam: Protein kinase domain
InterPro:
CATH:

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