› 4ae6

X-ray diffraction
2.1Å resolution

Structure and Function of the Human Sperm-Specific Isoform of Protein Kinase A (PKA) Catalytic Subunit Calpha 2

Released:
DOI: 10.2210/pdb4ae6/pdb
PDB entry 4ae6 coloured by chain, front view.
PDB entry 4ae6 coloured by chain, side view.
PDB entry 4ae6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and function of the human sperm-specific isoform of protein kinase A (PKA) catalytic subunit Cα2.
Hereng TH, Backe PH, Kahmann J, Scheich C, Bjørås M, Skålhegg BS, Rosendal KR
J Struct Biol 178 300-10 (2012)
PMID: 22504716

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148112 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cAMP-dependent protein kinase catalytic subunit alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 343 amino acids
Theoretical weight: 40.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P17612 (Residues: 10-351; Coverage: 97%)
  • Best match: P17612-2 (Residues: 1-343)
Gene names: PKACA, PRKACA
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ACT 1 x ACT
2 modified residues:
Ligand TPO 2 x TPO
Ligand SEP 2 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 75.776Å b: 89.495Å c: 114.815Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.215 0.283
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Sperm proteomics: road to male fertility and contraception.
Rahman et al. (2013)
1 more

1 mention without citation

A mechanism of global shape-dependent recognition and phosphorylation of filamin by protein kinase A.
Ithychanda et al. (2015)