› 3dak

X-ray diffraction
2.25Å resolution

Crystal Structure of Domain-Swapped OSR1 kinase domain

Released:
DOI: 10.2210/pdb3dak/pdb
PDB entry 3dak coloured by chain, front view.
PDB entry 3dak coloured by chain, side view.
PDB entry 3dak coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of domain-swapped STE20 OSR1 kinase domain.
Lee SJ, Cobb MH, Goldsmith EJ
Protein Sci 18 304-13 (2009)
PMID: 19177573

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132008 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase OSR1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 290 amino acids
Theoretical weight: 32.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95747 (Residues: 6-295; Coverage: 55%)
Gene names: KIAA1101, OSR1, OXSR1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ANP 4 x ANP
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P212121
Unit cell:
a: 74.208Å b: 104.484Å c: 162.903Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.195 0.267
Expression system: Escherichia coli

Quick links

Citations

7 review citations

The mammalian family of sterile 20p-like protein kinases.
Delpire E. (2009)
6 more

15 mentions without citation

Molecular physiology of SPAK and OSR1: two Ste20-related protein kinases regulating ion transport.
Gagnon et al. (2012)
14 more