X-ray diffraction
2.35Å resolution

Structure of serine hydroxymethyltransferase 8 from Glycine max cultivar Forrest complexed with PLP-Glycine


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 tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Serine hydroxymethyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 473 amino acids
Theoretical weight: 52.17 KDa
Source organism: Glycine max
Expression system: Escherichia coli
  • Canonical: K4FW35 (Residues: 1-471; Coverage: 100%)
Gene name: SHMT
Sequence domains: Serine hydroxymethyltransferase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Unit cell:
a: 55.727Å b: 127.445Å c: 127.733Å
α: 90° β: 90° γ: 90°
R R work R free
0.212 0.21 0.242
Expression system: Escherichia coli