Structure analysis

Human DRP-1 kinase, W305S S308A D40 mutant, crystal form with 8 monomers in the asymmetric unit

X-ray diffraction
3Å 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: 27897.98 Å2
Buried surface area: 3694.73 Å2
Dissociation area: 1,563.92 Å2
Dissociation energy (ΔGdiss): -6.74 kcal/mol
Dissociation entropy (TΔSdiss): 13.79 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-193792
Assembly 2
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Multimeric state: homo dimer
Accessible surface area: 27743.76 Å2
Buried surface area: 3638.15 Å2
Dissociation area: 1,535.45 Å2
Dissociation energy (ΔGdiss): -8.21 kcal/mol
Dissociation entropy (TΔSdiss): 13.78 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-193792
Assembly 3
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Multimeric state: homo dimer
Accessible surface area: 27772.75 Å2
Buried surface area: 3785.8 Å2
Dissociation area: 1,606.65 Å2
Dissociation energy (ΔGdiss): -5.29 kcal/mol
Dissociation entropy (TΔSdiss): 13.8 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-193792
Assembly 4
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Multimeric state: homo dimer
Accessible surface area: 27698.63 Å2
Buried surface area: 3878.72 Å2
Dissociation area: 1,657.15 Å2
Dissociation energy (ΔGdiss): -7.61 kcal/mol
Dissociation entropy (TΔSdiss): 13.81 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-193792

Macromolecules

Chains: A, B, C, D, E, F, G, H
Length: 321 amino acids
Theoretical weight: 37.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UIK4 (Residues: 11-330; Coverage: 87%)
Gene name: DAPK2
Pfam: Protein kinase domain
InterPro:
CATH:

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