6wct

X-ray diffraction
2.1Å resolution

Crystal structure of a guanylate kinase from Stenotrophomonas maltophilia K279a bound to guanosine-5'-monophosphate

Released:
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed:
ATP + GMP = ADP + GDP 
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Guanylate kinase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 229 amino acids
Theoretical weight: 25.21 KDa
Source organism: Stenotrophomonas maltophilia K279a
Expression system: Escherichia coli
UniProt:
  • Canonical: B2FT06 (Residues: 1-221; Coverage: 100%)
Gene names: Smlt3842, gmk
Sequence domains: Guanylate kinase

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P21
Unit cell:
a: 62.66Å b: 101.42Å c: 70.02Å
α: 90° β: 92.03° γ: 90°
R-values:
R R work R free
0.182 0.179 0.229
Expression system: Escherichia coli