4l0n

X-ray diffraction
1.4Å resolution

Crystal structure of STK3 (MST2) SARAH domain

Released:
Source organism: Homo sapiens
Entry authors: Chaikuad A, Krojer T, Newman JA, Dixon-Clarke S, von Delft F, Arrowsmith CH, Edwards AM, Bountra C, Knapp S, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-171593 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase 3 20kDa subunit Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 51 amino acids
Theoretical weight: 6.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13188 (Residues: 436-484; Coverage: 10%)
Gene names: KRS1, MST2, STK3
Sequence domains: C terminal SARAH domain of Mst1
Structure domains: p53-like tetramerisation domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P41212
Unit cell:
a: 61.32Å b: 61.32Å c: 301.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.16 0.207
Expression system: Escherichia coli BL21(DE3)