› 1yjz

X-ray diffraction
2.1Å resolution

K226M Mutant Of Serine Hydroxymethyltransferase From B. Stearothermophilus

Released:
DOI: 10.2210/pdb1yjz/pdb
PDB entry 1yjz coloured by chain, front view.
PDB entry 1yjz coloured by chain, side view.
PDB entry 1yjz coloured by chain, top view.
Source organism: Geobacillus stearothermophilus
Primary publication:
Role of Lys-226 in the catalytic mechanism of Bacillus stearothermophilus serine hydroxymethyltransferase--crystal structure and kinetic studies.
Bhavani S, Trivedi V, Jala VR, Subramanya HS, Kaul P, Prakash V, Appaji Rao N, Savithri HS
Biochemistry 44 6929-37 (2005)
PMID: 15865438

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 Chain: A
Molecule details ›
Chain: A
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 1 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21212
Unit cell:
a: 61.048Å b: 106.524Å c: 56.903Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.212 0.261
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

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