› 2vmu

X-ray diffraction
1.84Å resolution

Crystal structure of Y60AbsSHMT crystallized in the presence of L- allo-Thr

Released:
DOI: 10.2210/pdb2vmu/pdb
PDB entry 2vmu coloured by chain, front view.
PDB entry 2vmu coloured by chain, side view.
PDB entry 2vmu coloured by chain, top view.
Source organism: Geobacillus stearothermophilus
Primary publication:
Structural and functional studies of Bacillus stearothermophilus serine hydroxymethyltransferase: the role of Asn(341), Tyr(60) and Phe(351) in tetrahydrofolate binding.
Pai VR, Rajaram V, Bisht S, Bhavani BS, Rao NA, Murthy MR, Savithri HS
Biochem J 418 635-42 (2009)
PMID: 19046138

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: 44.18 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: 61.281Å b: 106.571Å c: 57.19Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.195 0.227
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

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