› 7loo

X-ray diffraction
1.95Å resolution

S-adenosyl methionine transferase cocrystallized with ATP

Released:
DOI: 10.2210/pdb7loo/pdb
PDB entry 7loo coloured by chain, front view.
PDB entry 7loo coloured by chain, side view.
PDB entry 7loo coloured by chain, top view.
Source organism: Escherichia coli 908573
Primary publication:
Substrate Dynamics Contribute to Enzymatic Specificity in Human and Bacterial Methionine Adenosyltransferases.
Gade M, Tan LL, Damry AM, Sandhu M, Brock JS, Delaney A, Villar-Briones A, Jackson CJ, Laurino P
OpenAccess logo JACS Au 1 2349-2360 (2021)
PMID: 34977903

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-241571 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
S-adenosylmethionine synthase Chains: A, B, Q, R
Molecule details ›
Chains: A, B, Q, R
Length: 384 amino acids
Theoretical weight: 42 KDa
Source organism: Escherichia coli 908573
Expression system: Escherichia coli BL21(DE3)

Ligands and Environments

6 bound ligands:
Ligand POP 4 x POP
Ligand PO4 4 x PO4
Ligand MG 8 x MG
Ligand K 4 x K
Ligand EDO 9 x EDO
Ligand SAM 6 x SAM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P21
Unit cell:
a: 67.922Å b: 117.78Å c: 113.21Å
α: 90° β: 107.519° γ: 90°
R-values:
R R work R free
0.172 0.17 0.207
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Mechanisms of protein evolution.
Jayaraman et al. (2022)
2 other articles