› 6qyx

X-ray diffraction
1.66Å resolution

p38(alpha) MAP kinase with the activation loop of ERK2

Released:
DOI: 10.2210/pdb6qyx/pdb
PDB entry 6qyx coloured by chain, front view.
PDB entry 6qyx coloured by chain, side view.
PDB entry 6qyx coloured by chain, top view.
Source organisms:
Primary publication:
The bacterial metalloprotease NleD selectively cleaves mitogen-activated protein kinases that have high flexibility in their activation loop.
Gur-Arie L, Eitan-Wexler M, Weinberger N, Rosenshine I, Livnah O
J Biol Chem 295 9409-9420 (2020)
PMID: 32404367

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-112347 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitogen-activated protein kinase 14; mitogen-activated protein kinase Chain: A
Molecule details ›
Chain: A
Length: 366 amino acids
Theoretical weight: 41.98 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: Q16539 (Residues: 1-166, 197-360; Coverage: 92%)
  • Canonical: D2CIU1 (Residues: 12-47; Coverage: 25%)
Gene names: CSBP, CSBP1, CSBP2, CSPB1, MAPK14, MXI2, SAPK2A
Sequence domains: Protein kinase domain

Ligands and Environments

2 bound ligands:
Ligand BOG 1 x BOG
Ligand EPE 1 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 68.86Å b: 74.5Å c: 75.28Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.185 0.242
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Interesting Biochemistries in the Structure and Function of Bacterial Effectors.
Mak et al. (2021)
3 more

1 mention without citation

The bacterial metalloprotease NleD selectively cleaves mitogen-activated protein kinases that have high flexibility in their activation loop.
Gur-Arie et al. (2020)