› 1ql6

X-ray diffraction
2.4Å resolution

THE CATALYTIC MECHANISM OF PHOSPHORYLASE KINASE PROBED BY MUTATIONAL STUDIES

Released:
DOI: 10.2210/pdb1ql6/pdb
PDB entry 1ql6 coloured by chain, front view.
PDB entry 1ql6 coloured by chain, side view.
PDB entry 1ql6 coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Catalytic mechanism of phosphorylase kinase probed by mutational studies.
Skamnaki VT, Owen DJ, Noble ME, Lowe ED, Lowe G, Oikonomakos NG, Johnson LN
Biochemistry 38 14718-30 (1999)
PMID: 10545198

Function and Biology Details

Reactions catalysed: 
ATP + a protein = ADP + a phosphoprotein
2 ATP + phosphorylase b = 2 ADP + phosphorylase a
ATP + [tau protein] = ADP + [tau protein] phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132600 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform Chain: A
Molecule details ›
Chain: A
Length: 298 amino acids
Theoretical weight: 34.27 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00518 (Residues: 2-299; Coverage: 77%)
Gene names: PHKG, PHKG1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ATP 1 x ATP
Ligand MN 2 x MN
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF
Spacegroup: P212121
Unit cell:
a: 47.56Å b: 68.171Å c: 112.475Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.24 0.33
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Regulation of protein kinases; controlling activity through activation segment conformation.
Nolen et al. (2004)
4 more

3 mentions without citation

A targeted library screen reveals a new inhibitor scaffold for protein kinase D.
Tandon et al. (2012)
2 more