Function and Biology Details
Reaction catalysed:
Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184053 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase class A catalytic domain-containing protein
Molecule details ›
Chains: A, B, C, D
Length: 298 amino acids
Theoretical weight: 32.8 KDa
Source organism: Synechococcus elongatus
Expression system: Escherichia coli
UniProt:
Sequence domains: Beta-lactamase enzyme family
Structure domains: DD-peptidase/beta-lactamase superfamily
Length: 298 amino acids
Theoretical weight: 32.8 KDa
Source organism: Synechococcus elongatus
Expression system: Escherichia coli
UniProt:
- Canonical:
Q8DH45 (Residues: 93-368; Coverage: 75%)
Sequence domains: Beta-lactamase enzyme family
Structure domains: DD-peptidase/beta-lactamase superfamily
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup:
P212121
Expression system: Escherichia coli
