› 4zsg

X-ray diffraction
1.79Å resolution

MITOGEN ACTIVATED PROTEIN KINASE 7 IN COMPLEX WITH INHIBITOR

Released:
DOI: 10.2210/pdb4zsg/pdb
PDB entry 4zsg coloured by chain, front view.
PDB entry 4zsg coloured by chain, side view.
PDB entry 4zsg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Discovery of a novel allosteric inhibitor-binding site in ERK5: comparison with the canonical kinase hinge ATP-binding site.
Chen H, Tucker J, Wang X, Gavine PR, Phillips C, Augustin MA, Schreiner P, Steinbacher S, Preston M, Ogg D
Acta Crystallogr D Struct Biol 72 682-93 (2016)
PMID: 27139631

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-171583 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitogen-activated protein kinase 7 Chain: A
Molecule details ›
Chain: A
Length: 347 amino acids
Theoretical weight: 39.76 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q13164 (Residues: 47-393; Coverage: 43%)
Gene names: BMK1, ERK5, MAPK7, PRKM7
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GOL 5 x GOL
Ligand 4QX 1 x 4QX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P41212
Unit cell:
a: 92.53Å b: 92.53Å c: 107.48Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.204 0.235
Expression system: Spodoptera frugiperda

Quick links

Citations

1 review citation

Small molecule ERK5 kinase inhibitors paradoxically activate ERK5 signalling: be careful what you wish for….
Cook et al. (2020)
7 other articles

4 mentions without citation

Quercetin conjugated with superparamagnetic iron oxide nanoparticles improves learning and memory better than free quercetin via interacting with proteins involved in LTP.
Amanzadeh et al. (2019)
3 more