PDBe 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:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (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:

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