› 2am2

X-ray diffraction
2.8Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + D-alanyl-D-alanine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184119 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase Chain: A
Molecule details ›
Chain: A
Length: 454 amino acids
Theoretical weight: 50.75 KDa
Source organism: Streptococcus pneumoniae R6
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8DNV6 (Residues: 1-454; Coverage: 99%)
Gene names: murF, spr1514
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 2LG 1 x 2LG
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6122
Unit cell:
a: 116.624Å b: 116.624Å c: 162.91Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.243 0.243 0.318
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Cytoplasmic steps of peptidoglycan biosynthesis.
Barreteau et al. (2008)
8 more

1 mention without citation

Structure of MurF from Streptococcus pneumoniae co-crystallized with a small molecule inhibitor exhibits interdomain closure.
Longenecker et al. (2005)