› 7q00

X-ray diffraction
1.74Å resolution

Crystal structure of serine hydroxymethyltransferase, isoform 4 from Arabidopsis thaliana (SHM4)

Released:
DOI: 10.2210/pdb7q00/pdb
PDB entry 7q00 coloured by chain, front view.
PDB entry 7q00 coloured by chain, side view.
PDB entry 7q00 coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Arabidopsis thaliana serine hydroxymethyltransferases: functions, structures, and perspectives.
Nogués I, Sekula B, Angelaccio S, Grzechowiak M, Tramonti A, Contestabile R, Ruszkowski M
Plant Physiol Biochem 187 37-49 (2022)
PMID: 35947902

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 tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127649 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine hydroxymethyltransferase 4 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 474 amino acids
Theoretical weight: 52.28 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: O23254 (Residues: 1-471; Coverage: 100%)
Gene names: At4g13930, FCAALL.160, SHM4, SHMT4, dl3005c
Sequence domains: Serine hydroxymethyltransferase

Ligands and Environments

2 bound ligands:
Ligand EDO 6 x EDO
Ligand TRS 1 x TRS
1 modified residue:
Ligand LLP 4 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 59.091Å b: 130.914Å c: 121.778Å
α: 90° β: 92.261° γ: 90°
R-values:
R R work R free
0.162 0.162 0.201
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Quick links

Citations

1 citations in other articles

New insights into the regulation of plant metabolism by O-acetylserine: sulfate and beyond.
Apodiakou et al. (2023)