› 5a1g

X-ray diffraction
1.83Å resolution

The structure of Human MAT2A in complex with S-adenosylethionine and PPNP.

Released:
DOI: 10.2210/pdb5a1g/pdb
PDB entry 5a1g coloured by chain, front view.
PDB entry 5a1g coloured by chain, side view.
PDB entry 5a1g coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystallography captures catalytic steps in human methionine adenosyltransferase enzymes.
Murray B, Antonyuk SV, Marina A, Lu SC, Mato JM, Hasnain SS, Rojas AL
Proc Natl Acad Sci U S A 113 2104-9 (2016)
PMID: 26858410

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 Chain: A
Molecule details ›
Chain: A
Length: 395 amino acids
Theoretical weight: 43.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
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

6 bound ligands:
Ligand MPD 2 x MPD
Ligand PPK 1 x PPK
Ligand IMD 1 x IMD
Ligand S7M 1 x S7M
Ligand K 1 x K
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: I222
Unit cell:
a: 68.39Å b: 94.39Å c: 117.39Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.122 0.12 0.175
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

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

3 mentions without citation

Crystallography captures catalytic steps in human methionine adenosyltransferase enzymes.
Murray et al. (2016)
2 more