› 3g8m

X-ray diffraction
3.3Å resolution

Serine Hydroxymethyltransferase Y55F Mutant

Released:
DOI: 10.2210/pdb3g8m/pdb
PDB entry 3g8m coloured by chain, front view.
PDB entry 3g8m coloured by chain, side view.
PDB entry 3g8m coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Role of a conserved active site cation-pi interaction in Escherichia coli serine hydroxymethyltransferase.
Vivoli M, Angelucci F, Ilari A, Morea V, Angelaccio S, di Salvo ML, Contestabile R
Biochemistry 48 12034-46 (2009)
PMID: 19883126

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-141655 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine hydroxymethyltransferase Chain: A
Molecule details ›
Chain: A
Length: 417 amino acids
Theoretical weight: 45.36 KDa
Source organism: Escherichia coli K-12
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 PLP 1 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P41212
Unit cell:
a: 112.59Å b: 112.59Å c: 68.929Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.256 0.255 0.275
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

1 mention without citation

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