PDBe 1jwq

X-ray diffraction
1.8Å resolution

Structure of the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus

Released:
Source organism: Paenibacillus polymyxa
Entry authors: Yamane T, Koyama Y, Nojiri Y, Hikage T, Akita M, Suzuki A, Shirai T, Ise F, Shida T, Sekiguchi J

Function and Biology Details

Reaction catalysed:
Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. 
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CwlV Chain: A
Molecule details ›
Chain: A
Length: 179 amino acids
Theoretical weight: 19.71 KDa
Source organism: Paenibacillus polymyxa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9LCR3 (Residues: 322-499; Coverage: 37%)
Gene name: cwlV
Sequence domains: N-acetylmuramoyl-L-alanine amidase
Structure domains: Zn-dependent exopeptidases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P61
Unit cell:
a: 66.5Å b: 66.5Å c: 88.34Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.176 0.206
Expression system: Escherichia coli