› 2uv2

X-ray diffraction
2.3Å resolution

Crystal Structure Of Human Ste20-Like Kinase Bound To 4-(4-(5- Cyclopropyl-1H-pyrazol-3-ylamino)-quinazolin-2-ylamino)-phenyl)- acetonitrile

Released:
DOI: 10.2210/pdb2uv2/pdb
PDB entry 2uv2 coloured by chain, front view.
PDB entry 2uv2 coloured by chain, side view.
PDB entry 2uv2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites.
Pike AC, Rellos P, Niesen FH, Turnbull A, Oliver AW, Parker SA, Turk BE, Pearl LH, Knapp S
EMBO J 27 704-14 (2008)
PMID: 18239682

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190547 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
STE20-like serine/threonine-protein kinase Chain: A
Molecule details ›
Chain: A
Length: 325 amino acids
Theoretical weight: 37.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9H2G2 (Residues: 12-15, 16-320; Coverage: 25%)
Gene names: KIAA0204, SLK, STK2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand EDO 5 x EDO
Ligand SCN 2 x SCN
Ligand GVD 1 x GVD
1 modified residue:
Ligand TPO 1 x TPO

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P6122
Unit cell:
a: 101.26Å b: 101.26Å c: 176.471Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.198 0.234
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

17 review citations

The structural basis for control of eukaryotic protein kinases.
Endicott et al. (2012)
16 more

2 mentions without citation

Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites.
Pike et al. (2008)
1 more