X-ray diffraction
2.86Å resolution

Crystal structure of RIP1 kinase in complex with necrostatin-3 analog

Source organism: Homo sapiens
Primary publication:
Structural Basis of RIP1 Inhibition by Necrostatins.
Structure 21 493-9 (2013)
PMID: 23473668

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Receptor-interacting serine/threonine-protein kinase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 294 amino acids
Theoretical weight: 33.47 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
  • Canonical: Q13546 (Residues: 1-294; Coverage: 44%)
Gene names: RIP, RIP1, RIPK1
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 82.63Å b: 91.407Å c: 103.325Å
α: 90° β: 90° γ: 90°
R R work R free
0.229 0.227 0.266
Expression system: Spodoptera frugiperda