› 1zmu

X-ray diffraction
2.9Å resolution

Catalytic and ubiqutin-associated domains of MARK2/PAR-1: Wild type

Released:
DOI: 10.2210/pdb1zmu/pdb
PDB entry 1zmu coloured by chain, front view.
PDB entry 1zmu coloured by chain, side view.
PDB entry 1zmu coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structure of the catalytic and ubiquitin-associated domains of the protein kinase MARK/Par-1.
Panneerselvam S, Marx A, Mandelkow EM, Mandelkow E
Structure 14 173-83 (2006)
PMID: 16472737

Function and Biology Details

Reactions catalysed: 
ATP + a protein = ADP + a phosphoprotein
ATP + [tau protein] = ADP + [tau protein] phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126652 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase MARK2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 327 amino acids
Theoretical weight: 37.65 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O08679 (Residues: 39-364; Coverage: 45%)
Gene name: Mark2
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P61
Unit cell:
a: 120.269Å b: 120.269Å c: 99.533Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.195 0.27
Expression system: Escherichia coli

Quick links

Citations

15 review citations

AMPK in Health and Disease.
Steinberg et al. (2009)
14 more

3 mentions without citation

Substrate and docking interactions in serine/threonine protein kinases.
Goldsmith et al. (2007)
2 more