› 1dfo

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE AT 2.4 ANGSTROM RESOLUTION OF E. COLI SERINE HYDROXYMETHYLTRANSFERASE IN COMPLEX WITH GLYCINE AND 5-FORMYL TETRAHYDROFOLATE

Released:
DOI: 10.2210/pdb1dfo/pdb
PDB entry 1dfo coloured by chain, front view.
PDB entry 1dfo coloured by chain, side view.
PDB entry 1dfo coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure at 2.4 A resolution of E. coli serine hydroxymethyltransferase in complex with glycine substrate and 5-formyl tetrahydrofolate.
Scarsdale JN, Radaev S, Kazanina G, Schirch V, Wright HT
J Mol Biol 296 155-68 (2000)
PMID: 10656824

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 domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141655 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine hydroxymethyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 417 amino acids
Theoretical weight: 45.37 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A825 (Residues: 1-417; Coverage: 100%)
Gene names: JW2535, b2551, glyA
Sequence domains: Serine hydroxymethyltransferase
Structure domains:

Ligands and Environments


Cofactor: Ligand FFO 4 x FFO
1 bound ligand:
Ligand PLG 4 x PLG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 77.46Å b: 172.24Å c: 95.05Å
α: 90° β: 104.12° γ: 90°
R-values:
R R work R free
0.174 0.174 0.196
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Serine hydroxymethyltransferase revisited.
Schirch et al. (2005)
1 more

20 mentions without citation

Threonine aldolases: perspectives in engineering and screening the enzymes with enhanced substrate and stereo specificities.
Fesko K. (2016)
19 more