› 6c9d

X-ray diffraction
2.5Å resolution

Crystal structure of KA1-autoinhibited MARK1 kinase

Released:
DOI: 10.2210/pdb6c9d/pdb
PDB entry 6c9d coloured by chain, front view.
PDB entry 6c9d coloured by chain, side view.
PDB entry 6c9d coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Basis for MARK1 Kinase Autoinhibition by Its KA1 Domain.
Emptage RP, Lemmon MA, Ferguson KM, Marmorstein R
Structure 26 1137-1143.e3 (2018)
PMID: 30099988

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192798 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase MARK1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 459 amino acids
Theoretical weight: 52.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9P0L2 (Residues: 45-795; Coverage: 57%)
Gene names: KIAA1477, MARK, MARK1
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2
Unit cell:
a: 169.993Å b: 69.578Å c: 103.999Å
α: 90° β: 124.3° γ: 90°
R-values:
R R work R free
0.206 0.203 0.251
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Allosteric regulation and inhibition of protein kinases.
Mingione et al. (2023)
6 other articles

3 mentions without citation

Root angle in maize influences nitrogen capture and is regulated by calcineurin B-like protein (CBL)-interacting serine/threonine-protein kinase 15 (ZmCIPK15).
Schneider et al. (2022)
2 more