› 1kl2

X-ray diffraction
2.7Å resolution

Crystal Structure of Serine Hydroxymethyltransferase Complexed with Glycine and 5-formyl tetrahydrofolate

Released:
DOI: 10.2210/pdb1kl2/pdb
PDB entry 1kl2 coloured by chain, front view.
PDB entry 1kl2 coloured by chain, side view.
PDB entry 1kl2 coloured by chain, top view.
Source organism: Geobacillus stearothermophilus
Primary publication:
Crystal structure of binary and ternary complexes of serine hydroxymethyltransferase from Bacillus stearothermophilus: insights into the catalytic mechanism.
Trivedi V, Gupta A, Jala VR, Saravanan P, Rao GS, Rao NA, Savithri HS, Subramanya HS
J Biol Chem 277 17161-9 (2002)
PMID: 11877399

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-181944 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine hydroxymethyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 419 amino acids
Theoretical weight: 45.71 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7SIB6 (Residues: 1-419; Coverage: 100%)
Gene name: glyA
Sequence domains: Serine hydroxymethyltransferase
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP

Cofactor: Ligand FON 2 x FON
1 bound ligand:
Ligand GLY 2 x GLY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 57.419Å b: 104.609Å c: 62.489Å
α: 90° β: 91.43° γ: 90°
R-values:
R R work R free
0.208 0.208 0.236
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Serine hydroxymethyltransferase revisited.
Schirch et al. (2005)
30 other articles

7 mentions without citation

Extremophilic SHMTs: from structure to biotechnology.
Angelaccio S. (2013)
6 more