› 5yg3

X-ray diffraction
2.4Å 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-103455 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
glycine hydroxymethyltransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 442 amino acids
Theoretical weight: 49.25 KDa
Source organism: Plasmodium vivax
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A1G4H5I1 (Residues: 1-442; Coverage: 100%)
Gene names: PVC01_140059500, PVP01_1453700, PVT01_140059000, PVW1_140060100
Sequence domains: Serine hydroxymethyltransferase

Ligands and Environments

3 bound ligands:
Ligand PLG 3 x PLG
Ligand 8UC 3 x 8UC
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER D8 QUEST
Spacegroup: C2
Unit cell:
a: 101.623Å b: 58.727Å c: 236.139Å
α: 90° β: 90.32° γ: 90°
R-values:
R R work R free
0.23 0.222 0.3
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Dihydrofolate reductase, thymidylate synthase, and serine hydroxy methyltransferase: successful targets against some infectious diseases.
Shamshad et al. (2022)
7 other articles