4oxd

X-ray diffraction
2.8Å resolution

Structure of the LdcB LD-carboxypeptidase reveals the molecular basis of peptidoglycan recognition

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
monomeric
PDBe Complex ID:
PDB-CPX-164961 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidase M15B domain-containing protein Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 187 amino acids
Theoretical weight: 21.2 KDa
Source organism: Streptococcus pneumoniae R6
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8DQQ1 (Residues: 56-238; Coverage: 84%)
Gene name: spr0554
Sequence domains: D-alanyl-D-alanine carboxypeptidase
Structure domains: Muramoyl-pentapeptide Carboxypeptidase; domain 2
MUB-ALA-ZGL-LYS-DSG Chain: H
Molecule details ›
Chain: H
Length: 4 amino acids
Theoretical weight: 461 Da
Source organism: Lactobacillus acidophilus

Ligands and Environments

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: C2
Unit cell:
a: 345.954Å b: 42.549Å c: 79.318Å
α: 90° β: 93.07° γ: 90°
R-values:
R R work R free
0.276 0.273 0.334
Expression system: Escherichia coli