› 5bv6

X-ray diffraction
1.94Å resolution

PKG II's Carboxyl Terminal Cyclic Nucleotide Binding Domain (CNB-B) in a complex with cGMP

Released:
DOI: 10.2210/pdb5bv6/pdb
PDB entry 5bv6 coloured by chain, front view.
PDB entry 5bv6 coloured by chain, side view.
PDB entry 5bv6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Basis of Cyclic Nucleotide Selectivity in cGMP-dependent Protein Kinase II.
Campbell JC, Kim JJ, Li KY, Huang GY, Reger AS, Matsuda S, Sankaran B, Link TM, Yuasa K, Ladbury JE, Casteel DE, Kim C
J Biol Chem 291 5623-5633 (2016)
PMID: 26769964

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171613 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cGMP-dependent protein kinase 2 Chain: A
Molecule details ›
Chain: A
Length: 152 amino acids
Theoretical weight: 17.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13237 (Residues: 269-418; Coverage: 20%)
Gene names: PRKG2, PRKGR2
Sequence domains: Cyclic nucleotide-binding domain
Structure domains: Jelly Rolls

Ligands and Environments

4 bound ligands:
Ligand 35G 1 x 35G
Ligand CA 2 x CA
Ligand ACT 1 x ACT
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P212121
Unit cell:
a: 40.344Å b: 50.479Å c: 69.167Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.177 0.211
Expression system: Escherichia coli

Quick links

Citations

7 citation in other articles

Structures of the cGMP-dependent protein kinase in malaria parasites reveal a unique structural relay mechanism for activation.
El Bakkouri et al. (2019)
6 more

6 mentions without citation

Cyclic nucleotide selectivity of protein kinase G isozymes.
Kim et al. (2021)
5 more