› 1lvg

X-ray diffraction
2.1Å resolution

Crystal structure of mouse guanylate kinase in complex with GMP and ADP

Released:
DOI: 10.2210/pdb1lvg/pdb
PDB entry 1lvg coloured by chain, front view.
PDB entry 1lvg coloured by chain, side view.
PDB entry 1lvg coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural characterization of the closed conformation of mouse guanylate kinase.
Sekulic N, Shuvalova L, Spangenberg O, Konrad M, Lavie A
J Biol Chem 277 30236-43 (2002)
PMID: 12036965

Function and Biology Details

Reaction catalysed: 
ATP + GMP = ADP + GDP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179144 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Guanylate kinase Chain: A
Molecule details ›
Chain: A
Length: 198 amino acids
Theoretical weight: 21.95 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q64520 (Residues: 1-198; Coverage: 100%)
Gene names: Gmk, Guk1
Sequence domains: Guanylate kinase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand K 1 x K
Ligand ADP 1 x ADP
Ligand 5GP 1 x 5GP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P41212
Unit cell:
a: 67.241Å b: 67.241Å c: 108.696Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.231
Expression system: Escherichia coli BL21

Quick links

Citations

37 citation in other articles

Structural analysis of the voltage-dependent calcium channel beta subunit functional core and its complex with the alpha 1 interaction domain.
Opatowsky et al. (2004)
36 more

15 mentions without citation

DynaMut2: Assessing changes in stability and flexibility upon single and multiple point missense mutations.
Rodrigues et al. (2021)
14 more