› 5hez

X-ray diffraction
2.66Å resolution

JAK2 kinase (JH1 domain) mutant P1057A in complex with TG101209

Released:
DOI: 10.2210/pdb5hez/pdb
PDB entry 5hez coloured by chain, front view.
PDB entry 5hez coloured by chain, side view.
PDB entry 5hez coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Resolving TYK2 locus genotype-to-phenotype differences in autoimmunity.
Dendrou CA, Cortes A, Shipman L, Evans HG, Attfield KE, Jostins L, Barber T, Kaur G, Kuttikkatte SB, Leach OA, Desel C, Faergeman SL, Cheeseman J, Neville MJ, Sawcer S, Compston A, Johnson AR, Everett C, Bell JI, Karpe F, Ultsch M, Eigenbrot C, McVean G, Fugger L
Sci Transl Med 8 363ra149 (2016)
PMID: 27807284

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

Assemblies composition:
monomeric (preferred)
homo octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-130063 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase JAK2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 302 amino acids
Theoretical weight: 35.46 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O60674 (Residues: 833-1132; Coverage: 27%)
Gene name: JAK2
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand CL 3 x CL
Ligand ZN 2 x ZN
Ligand 1M3 8 x 1M3
1 modified residue:
Ligand PTR 8 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: C222
Unit cell:
a: 211.813Å b: 215.649Å c: 91.497Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.217 0.238
Expression system: Spodoptera frugiperda

Quick links

Citations

54 review citations

A brief history of human disease genetics.
Claussnitzer et al. (2020)
53 more

2 mentions without citation

Creation of artificial protein-protein interactions using α-helices as interfaces.
Yagi et al. (2018)
1 more