› 4m0y

X-ray diffraction
1.7Å resolution

Crystal structure of ITK in complex with compound 1 [4-(carbamoylamino)-1-(naphthalen-1-yl)-1H-pyrazole-3-carboxamide]

Released:
DOI: 10.2210/pdb4m0y/pdb
PDB entry 4m0y coloured by chain, front view.
PDB entry 4m0y coloured by chain, side view.
PDB entry 4m0y coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Selectively targeting an inactive conformation of interleukin-2-inducible T-cell kinase by allosteric inhibitors.
Han S, Czerwinski RM, Caspers NL, Limburg DC, Ding W, Wang H, Ohren JF, Rajamohan F, McLellan TJ, Unwalla R, Choi C, Parikh MD, Seth N, Edmonds J, Phillips C, Shakya S, Li X, Spaulding V, Hughes S, Cook A, Robinson C, Mathias JP, Navratilova I, Medley QG, Anderson DR, Kurumbail RG, Aulabaugh A
Biochem J 460 211-22 (2014)
PMID: 24593284

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170703 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase ITK/TSK Chain: A
Molecule details ›
Chain: A
Length: 269 amino acids
Theoretical weight: 30.65 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q08881 (Residues: 354-620; Coverage: 43%)
Gene names: EMT, ITK, LYK
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand M0Y 2 x M0Y
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P21
Unit cell:
a: 41.075Å b: 69.084Å c: 49.952Å
α: 90° β: 106.59° γ: 90°
R-values:
R R work R free
0.192 0.19 0.217
Expression system: Spodoptera frugiperda

Quick links

Citations

2 review citations

Structure-Function Relationships of Covalent and Non-Covalent BTK Inhibitors.
Zain et al. (2021)
1 more

8 mentions without citation

Discovery of a novel allosteric inhibitor-binding site in ERK5: comparison with the canonical kinase hinge ATP-binding site.
Chen et al. (2016)
7 more