› 4qtd

X-ray diffraction
1.5Å resolution

Structure of human JNK1 in complex with SCH772984 and the AMPPNP-hydrolysed triphosphate revealing the second type-I binding mode

Released:
DOI: 10.2210/pdb4qtd/pdb
PDB entry 4qtd coloured by chain, front view.
PDB entry 4qtd coloured by chain, side view.
PDB entry 4qtd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A unique inhibitor binding site in ERK1/2 is associated with slow binding kinetics.
Chaikuad A, Tacconi EM, Zimmer J, Liang Y, Gray NS, Tarsounas M, Knapp S
Nat Chem Biol 10 853-60 (2014)
PMID: 25195011

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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155379 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitogen-activated protein kinase 8 Chain: A
Molecule details ›
Chain: A
Length: 364 amino acids
Theoretical weight: 42.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P45983 (Residues: 1-363; Coverage: 85%)
Gene names: JNK1, MAPK8, PRKM8, SAPK1, SAPK1C
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand EDO 22 x EDO
Ligand EPE 1 x EPE
Ligand 38Z 1 x 38Z
Ligand ANP 1 x ANP
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 50.95Å b: 71.55Å c: 108.17Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.166 0.192
Expression system: Escherichia coli BL21

Quick links

Citations

19 review citations

Targeting RAS-ERK signalling in cancer: promises and challenges.
Samatar et al. (2014)
18 more

13 mentions without citation

A Perspective on the Development of c-Jun N-terminal Kinase Inhibitors as Therapeutics for Alzheimer's Disease: Investigating Structure through Docking Studies.
Cho et al. (2021)
12 more