› 3aln

X-ray diffraction
2.3Å resolution

Crystal Structure of human non-phosphorylated MKK4 kinase domain complexed with AMP-PNP

Released:
DOI: 10.2210/pdb3aln/pdb
PDB entry 3aln coloured by chain, front view.
PDB entry 3aln coloured by chain, side view.
PDB entry 3aln coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of MKK4 kinase domain reveal that substrate peptide binds to an allosteric site and induces an auto-inhibition state.
Matsumoto T, Kinoshita T, Kirii Y, Yokota K, Hamada K, Tada T
Biochem Biophys Res Commun 400 369-73 (2010)
PMID: 20732303

Function and Biology Details

Reaction catalysed: 
ATP + L-seryl/L-threonyl/L-tyrosyl-[protein] = ADP + O-phospho-L-seryl/O-phospho-L-threonyl/O-phospho-L-tyrosyl-[protein]
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155394 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity mitogen-activated protein kinase kinase 4 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 327 amino acids
Theoretical weight: 37.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P45985 (Residues: 80-399; Coverage: 80%)
Gene names: JNKK1, MAP2K4, MEK4, MKK4, PRKMK4, SEK1, SERK1, SKK1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ANP 3 x ANP
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P212121
Unit cell:
a: 66.508Å b: 76.123Å c: 173.126Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.289 0.284 0.378
Expression system: Escherichia coli

Quick links

Citations

5 review citations

JNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships.
Zeke et al. (2016)
4 more

14 mentions without citation

Kinase Atlas: Druggability Analysis of Potential Allosteric Sites in Kinases.
Yueh et al. (2019)
13 more