› 1phk

X-ray diffraction
2.2Å resolution

TWO STRUCTURES OF THE CATALYTIC DOMAIN OF PHOSPHORYLASE, KINASE: AN ACTIVE PROTEIN KINASE COMPLEXED WITH NUCLEOTIDE, SUBSTRATE-ANALOGUE AND PRODUCT

Released:
DOI: 10.2210/pdb1phk/pdb
PDB entry 1phk coloured by chain, front view.
PDB entry 1phk coloured by chain, side view.
PDB entry 1phk coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product.
Owen DJ, Noble ME, Garman EF, Papageorgiou AC, Johnson LN
Structure 3 467-82 (1995)
PMID: 7663944

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: 34.32 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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P212121
Unit cell:
a: 47.6Å b: 67.4Å c: 110.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.21 0.288
Expression system: Escherichia coli

Quick links

Citations

20 review citations

Active and inactive protein kinases: structural basis for regulation.
Johnson et al. (1996)
19 more

19 mentions without citation

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