› 5ekn

X-ray diffraction
2.59Å resolution

Crystal structure of MAPK13 complex with inhibitor

Released:
DOI: 10.2210/pdb5ekn/pdb
PDB entry 5ekn coloured by chain, front view.
PDB entry 5ekn coloured by chain, side view.
PDB entry 5ekn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
First comprehensive structural and biophysical analysis of MAPK13 inhibitors targeting DFG-in and DFG-out binding modes.
Yurtsever Z, Patel DA, Kober DL, Su A, Miller CA, Romero AG, Holtzman MJ, Brett TJ
Biochim Biophys Acta 1860 2335-2344 (2016)
PMID: 27369736

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127397 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitogen-activated protein kinase 13 Chain: A
Molecule details ›
Chain: A
Length: 371 amino acids
Theoretical weight: 42.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O15264 (Residues: 1-352; Coverage: 96%)
Gene names: MAPK13, PRKM13, SAPK4
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand N58 1 x N58
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P212121
Unit cell:
a: 61.047Å b: 70.206Å c: 92.908Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.218 0.273
Expression system: Escherichia coli

Quick links

Citations

6 review citations

p38γ and p38δ: From Spectators to Key Physiological Players.
Cuenda et al. (2017)
5 more

4 mentions without citation

First comprehensive structural and biophysical analysis of MAPK13 inhibitors targeting DFG-in and DFG-out binding modes.
Yurtsever et al. (2016)
3 more