› 4bj4

X-ray diffraction
1.72Å resolution

Function and Biology Details

Reaction catalysed: 
Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190918 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetylmuramoyl-L-alanine amidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 246 amino acids
Theoretical weight: 27.5 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9HT86 (Residues: 18-259; Coverage: 93%)
Gene names: PA5485, ampDh2
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand FLC 1 x FLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF
Spacegroup: P212121
Unit cell:
a: 48.759Å b: 100.421Å c: 104.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.172 0.201
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Lytic transglycosylases: concinnity in concision of the bacterial cell wall.
Dik et al. (2017)
6 more

2 mentions without citation

Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan.
Vermassen et al. (2019)
1 more