› 2vmw

X-ray diffraction
1.73Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181944 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine hydroxymethyltransferase Chain: A
Molecule details ›
Chain: A
Length: 405 amino acids
Theoretical weight: 44.18 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q7SIB6 (Residues: 1-405; Coverage: 97%)
Gene name: glyA
Sequence domains: Serine hydroxymethyltransferase
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
3 bound ligands:
Ligand SER 1 x SER
Ligand MPD 2 x MPD
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21212
Unit cell:
a: 61.118Å b: 106.39Å c: 57.205Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.179 0.211
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Extremophilic SHMTs: from structure to biotechnology.
Angelaccio S. (2013)
7 other articles

1 mention without citation

Chloroplastic Serine Hydroxymethyltransferase From Medicago truncatula: A Structural Characterization.
Ruszkowski et al. (2018)