› 4wxf

X-ray diffraction
2.4Å resolution

Crystal structure of L-Serine Hydroxymethyltransferase in complex with glycine

Released:
DOI: 10.2210/pdb4wxf/pdb
PDB entry 4wxf coloured by chain, front view.
PDB entry 4wxf coloured by chain, side view.
PDB entry 4wxf coloured by chain, top view.
Source organism: Streptococcus thermophilus CNRZ1066
Primary publication:
Engineered L-serine hydroxymethyltransferase from Streptococcus thermophilus for the synthesis of α,α-dialkyl-α-amino acids.
Hernandez K, Zelen I, Petrillo G, Usón I, Wandtke CM, Bujons J, Joglar J, Parella T, Clapés P
Angew Chem Int Ed Engl 54 3013-7 (2015)
PMID: 25611820

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-177580 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine hydroxymethyltransferase Chains: A, C
Molecule details ›
Chains: A, C
Length: 428 amino acids
Theoretical weight: 46.54 KDa
Source organism: Streptococcus thermophilus CNRZ1066
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5M0B4 (Residues: 1-416; Coverage: 100%)
Gene names: glyA, str0755
Sequence domains: Serine hydroxymethyltransferase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand PLG 2 x PLG
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P41212
Unit cell:
a: 115.47Å b: 115.47Å c: 191.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.158 0.204
Expression system: Escherichia coli

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Citations

3 review citations

Current Advances on Structure-Function Relationships of Pyridoxal 5'-Phosphate-Dependent Enzymes.
Liang et al. (2019)
2 more

1 mention without citation

Linear ubiquitin chains: enzymes, mechanisms and biology.
Rittinger et al. (2017)