Structure analysis

Crystal Structure of DAPK1 catalytic domain in complex with the hinge binding fragment 4-methylpyridazine

X-ray diffraction
1.4Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Multimeric state: monomeric
Accessible surface area: 14305.36 Å2
Buried surface area: 323.59 Å2
Dissociation area: 84.15 Å2
Dissociation energy (ΔGdiss): 10.76 kcal/mol
Dissociation entropy (TΔSdiss): 0.61 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-156788

Macromolecules

Chain: A
Length: 294 amino acids
Theoretical weight: 33.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53355 (Residues: 2-285; Coverage: 20%)
Gene names: DAPK, DAPK1
Pfam: Protein kinase domain
InterPro:
CATH:
PDBe-KB: UniProt Coverage View: P53355  
129420406080100120140160180200220240260280
 
100200
UniProt
P53355
Chains
Domains
Secondary structure
Flexibility predictions
Topology annotations
Early folding residue predictions
Ligand binding sites

Search similar proteins