› 2w7e

X-ray diffraction
1.69Å resolution

Crystal structure of Y51FbsSHMT obtained in the presence of Glycine

Released:
DOI: 10.2210/pdb2w7e/pdb
PDB entry 2w7e coloured by chain, front view.
PDB entry 2w7e coloured by chain, side view.
PDB entry 2w7e coloured by chain, top view.
Source organism: Geobacillus stearothermophilus
Primary publication:
Importance of tyrosine residues of Bacillus stearothermophilus serine hydroxymethyltransferase in cofactor binding and L-allo-Thr cleavage.
Bhavani BS, Rajaram V, Bisht S, Kaul P, Prakash V, Murthy MR, Appaji Rao N, Savithri HS
FEBS J 275 4606-19 (2008)
PMID: 18699779

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: 44.26 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 GLY 1 x GLY
Ligand MPD 1 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: 60.92Å b: 106.39Å c: 57.02Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.17 0.205
Expression system: Escherichia coli BL21

Quick links

Citations

6 citation in other articles

Mechanism for folate-independent aldolase reaction catalyzed by serine hydroxymethyltransferase.
Chiba et al. (2012)
5 more

1 mention without citation

Bioinformatic analysis of the fold type I PLP-dependent enzymes reveals determinants of reaction specificity in l-threonine aldolase from Aeromonas jandaei.
Fesko et al. (2018)