› 6fcd

X-ray diffraction
1.7Å resolution

Human Methionine Adenosyltransferase II mutant (R264A)

Released:
DOI: 10.2210/pdb6fcd/pdb
PDB entry 6fcd coloured by chain, front view.
PDB entry 6fcd coloured by chain, side view.
PDB entry 6fcd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Control and regulation of S-Adenosylmethionine biosynthesis by the regulatory β subunit and quinolone-based compounds.
Panmanee J, Bradley-Clarke J, Mato JM, O'Neill PM, Antonyuk SV, Hasnain SS
FEBS J 286 2135-2154 (2019)
PMID: 30776190

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
S-adenosylmethionine synthase isoform type-2 Chain: A
Molecule details ›
Chain: A
Length: 395 amino acids
Theoretical weight: 43.63 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

7 bound ligands:
Ligand MG 2 x MG
Ligand K 1 x K
Ligand PG4 1 x PG4
Ligand ADN 1 x ADN
Ligand PPV 1 x PPV
Ligand PEG 2 x PEG
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: I222
Unit cell:
a: 67.141Å b: 94.23Å c: 116.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.16 0.184
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)