› 6faj

X-ray diffraction
1.95Å resolution

The structure of Human Methionine Adenosyltransferase II in apo state

Released:
DOI: 10.2210/pdb6faj/pdb
PDB entry 6faj coloured by chain, front view.
PDB entry 6faj coloured by chain, side view.
PDB entry 6faj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Control and regulation of S-Adenosylmethionine biosynthesis by the regulatory beta subunit and quinolone-based compounds
Panmanee J, Bradley-Clarke J, Mato JM, O'Neill PM, Antonyuk SV, Hasnain SS
FEBS J. (2020)

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 tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151917 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
S-adenosylmethionine synthase isoform type-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 395 amino acids
Theoretical weight: 43.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P31153 (Residues: 1-395; Coverage: 100%)
Gene names: AMS2, MAT2A, MATA2
Sequence domains:
Structure domains: GMP Synthetase; Chain A, domain 3

Ligands and Environments

3 bound ligands:
Ligand PEG 2 x PEG
Ligand PG4 1 x PG4
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Unit cell:
a: 62.176Å b: 103.232Å c: 108.359Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.19 0.224
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Methionine adenosyltransferases in liver cancer.
Murray et al. (2019)
1 more

1 mention without citation

Control and regulation of S-Adenosylmethionine biosynthesis by the regulatory β subunit and quinolone-based compounds.
Panmanee et al. (2019)