PDBe 2j8y

X-ray diffraction
1.9Å resolution

Structure of PBP-A acyl-enzyme complex with penicillin-G

Released:

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tll2115 protein Chains: A, B, C, D
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:
  • Canonical: Q8DH45 (Residues: 93-368; Coverage: 75%)
Gene name: tll2115
Sequence domains: Beta-lactamase enzyme family
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P212121
Unit cell:
a: 87.692Å b: 91.873Å c: 147.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.187 0.245
Expression system: Escherichia coli