Function and Biology Details
Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171514 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase 4 18kDa subunit
Molecule details ›
Chain: A
Length: 51 amino acids
Theoretical weight: 6.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: C terminal SARAH domain of Mst1
Structure domains: p53-like tetramerisation domain
Length: 51 amino acids
Theoretical weight: 6.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
Q13043 (Residues: 432-480; Coverage: 10%)
Sequence domains: C terminal SARAH domain of Mst1
Structure domains: p53-like tetramerisation domain
Ras association domain-containing protein 5
Molecule details ›
Chain: B
Length: 55 amino acids
Theoretical weight: 6.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Novel Ras effector 1 C-terminal SARAH (Sav/Rassf/Hpo) domain
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 55 amino acids
Theoretical weight: 6.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical: Q8WWW0 (Residues: 366-418; Coverage: 13%)
Sequence domains: Novel Ras effector 1 C-terminal SARAH (Sav/Rassf/Hpo) domain
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
PHOTON FACTORY BEAMLINE BL-1A
Spacegroup:
C2221
Expression system: Escherichia coli BL21
