3gbx

X-ray diffraction
1.8Å resolution

Serine hydroxymethyltransferase from Salmonella typhimurium

Released:
Entry authors: Osipiuk J, Nocek B, Zhou M, Stam J, Anderson WF, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine hydroxymethyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 420 amino acids
Theoretical weight: 46.39 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A2E1 (Residues: 1-417; Coverage: 100%)
Gene names: STM2555, glyA
Sequence domains: Serine hydroxymethyltransferase
Structure domains:

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 73.955Å b: 49.734Å c: 94.736Å
α: 90° β: 110.67° γ: 90°
R-values:
R R work R free
0.154 0.152 0.191
Expression system: Escherichia coli