› 6es0

X-ray diffraction
2.38Å resolution

Crystal structure of the kinase domain of human RIPK2 in complex with the activation loop targeting inhibitor CS-R35

Released:
DOI: 10.2210/pdb6es0/pdb
PDB entry 6es0 coloured by chain, front view.
PDB entry 6es0 coloured by chain, side view.
PDB entry 6es0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Activation loop targeting strategy for design of receptor-interacting protein kinase 2 (RIPK2) inhibitors.
Suebsuwong C, Pinkas DM, Ray SS, Bufton JC, Dai B, Bullock AN, Degterev A, Cuny GD
Bioorg Med Chem Lett 28 577-583 (2018)
PMID: 29409752

Function and Biology Details

Reactions catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128905 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Receptor-interacting serine/threonine-protein kinase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 317 amino acids
Theoretical weight: 36.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43353 (Residues: 3-317; Coverage: 58%)
Gene names: CARDIAK, RICK, RIP2, RIPK2, UNQ277/PRO314/PRO34092
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains: Transferase(Phosphotransferase) domain 1

Ligands and Environments

1 bound ligand:
Ligand BW8 2 x BW8
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P212121
Unit cell:
a: 61.98Å b: 83.74Å c: 139.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.214 0.258
Expression system: Escherichia coli

Quick links

Citations

2 review citations

NOD Signaling and Cell Death.
Heim et al. (2019)
1 more

3 mentions without citation

Receptor-interacting protein kinase 2 (RIPK2) stabilizes c-Myc and is a therapeutic target in prostate cancer metastasis.
Yan et al. (2022)
2 more