› 1ls3

X-ray diffraction
2.7Å resolution

Crystal Structure of the Complex between Rabbit Cytosolic Serine Hydroxymethyltransferase and TriGlu-5-formyl-tetrahydrofolate

Released:
DOI: 10.2210/pdb1ls3/pdb
PDB entry 1ls3 coloured by chain, front view.
PDB entry 1ls3 coloured by chain, side view.
PDB entry 1ls3 coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.
Fu TF, Scarsdale JN, Kazanina G, Schirch V, Wright HT
J Biol Chem 278 2645-53 (2003)
PMID: 12438316

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 tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139606 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine hydroxymethyltransferase, cytosolic Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 483 amino acids
Theoretical weight: 52.92 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P07511 (Residues: 2-484; Coverage: 100%)
Gene name: SHMT1
Sequence domains: Serine hydroxymethyltransferase
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 4 x PLP
3 bound ligands:
Ligand GLY 2 x GLY
Ligand TGF 2 x TGF
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P41
Unit cell:
a: 114.084Å b: 114.084Å c: 156.719Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.22 0.294
Expression system: Escherichia coli

Quick links

Citations

11 citation in other articles

Cobalamin-independent methionine synthase (MetE): a face-to-face double barrel that evolved by gene duplication.
Pejchal et al. (2005)
10 more

11 mentions without citation

Human SHMT inhibitors reveal defective glycine import as a targetable metabolic vulnerability of diffuse large B-cell lymphoma.
Ducker et al. (2017)
10 more