› 3tr0

X-ray diffraction
1.85Å resolution

Structure of guanylate kinase (gmk) from Coxiella burnetii

Released:
DOI: 10.2210/pdb3tr0/pdb
PDB entry 3tr0 coloured by chain, front view.
PDB entry 3tr0 coloured by chain, side view.
PDB entry 3tr0 coloured by chain, top view.
Source organism: Coxiella burnetii
Primary publication:
Structural genomics for drug design against the pathogen Coxiella burnetii.
Franklin MC, Cheung J, Rudolph MJ, Burshteyn F, Cassidy M, Gary E, Hillerich B, Yao ZK, Carlier PR, Totrov M, Love JD
Proteins 83 2124-36 (2015)
PMID: 26033498

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182941 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Guanylate kinase Chain: A
Molecule details ›
Chain: A
Length: 205 amino acids
Theoretical weight: 23.77 KDa
Source organism: Coxiella burnetii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q83EL7 (Residues: 1-202; Coverage: 98%)
Gene names: CBU_0301, gmk
Sequence domains: Guanylate kinase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand 5GP 1 x 5GP
1 modified residue:
Ligand MSE 3 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2
Unit cell:
a: 67.834Å b: 45.899Å c: 70.042Å
α: 90° β: 90.35° γ: 90°
R-values:
R R work R free
0.194 0.191 0.233
Expression system: Escherichia coli BL21(DE3)

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Citations

5 review citations

Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology.
Martins et al. (2015)
4 more

1 mention without citation

Molecular mechanism and evolution of guanylate kinase regulation by (p)ppGpp.
Liu et al. (2015)