› 2am1

X-ray diffraction
2.5Å 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

2 bound ligands:
Ligand 1LG 1 x 1LG
Ligand GOL 1 x GOL
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6122
Unit cell:
a: 116.271Å b: 116.271Å c: 161.389Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.238 0.238 0.29
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

5 mentions without citation

Structural and functional features of enzymes of Mycobacterium tuberculosis peptidoglycan biosynthesis as targets for drug development.
Moraes et al. (2015)
4 more