› 6vcz

X-ray diffraction
1.52Å resolution

Crystal structure of Arabidopsis thaliana S-adenosylmethionine Synthase 2 (AtMAT2)

Released:
DOI: 10.2210/pdb6vcz/pdb
PDB entry 6vcz coloured by chain, front view.
PDB entry 6vcz coloured by chain, side view.
PDB entry 6vcz coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
S-adenosylmethionine synthases in plants: Structural characterization of type I and II isoenzymes from Arabidopsis thaliana and Medicago truncatula.
Sekula B, Ruszkowski M, Dauter Z
Int J Biol Macromol 151 554-565 (2020)
PMID: 32057875

Function and Biology Details

Reaction catalysed: 
ATP + L-methionine + H(2)O = phosphate + diphosphate + S-adenosyl-L-methionine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148087 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
S-adenosylmethionine synthase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 402 amino acids
Theoretical weight: 44.17 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P17562 (Residues: 1-392; Coverage: 100%)
Gene names: At4g01850, SAM2, T7B11.11
Sequence domains:

Ligands and Environments

6 bound ligands:
Ligand PO4 8 x PO4
Ligand MG 7 x MG
Ligand PGR 2 x PGR
Ligand MPO 1 x MPO
Ligand MXE 1 x MXE
Ligand PGE 2 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P21
Unit cell:
a: 62.798Å b: 99.276Å c: 86.93Å
α: 90° β: 109.74° γ: 90°
R-values:
R R work R free
0.16 0.16 0.18
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

C-H Groups as Donors in Hydrogen Bonds: A Historical Overview and Occurrence in Proteins and Nucleic Acids.
Derewenda ZS. (2023)
1 more

1 mention without citation

S-adenosylmethionine synthases in plants: Structural characterization of type I and II isoenzymes from Arabidopsis thaliana and Medicago truncatula.
Sekula et al. (2020)