2y2b

X-ray diffraction
1.9Å resolution

crystal structure of AmpD in complex with reaction products

Released:

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-160659 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 187 amino acids
Theoretical weight: 20.87 KDa
Source organism: Citrobacter freundii
Expression system: Escherichia coli
UniProt:
  • Canonical: P82974 (Residues: 1-187; Coverage: 100%)
Gene name: ampD
Sequence domains: N-acetylmuramoyl-L-alanine amidase
Structure domains: Peptidoglycan recognition protein-like

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P32
Unit cell:
a: 67.774Å b: 67.774Å c: 92.836Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.173 0.17 0.224
Expression system: Escherichia coli