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:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Probable peptidoglycan D,D-transpeptidase PenA (preferred)
PDBe Complex ID:
PDB-CPX-139932 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable peptidoglycan D,D-transpeptidase PenA
Molecule details ›
Chains: A, B
Length: 330 amino acids
Theoretical weight: 35.41 KDa
Source organism: Neisseria gonorrhoeae FA6140
Expression system: Escherichia coli
UniProt:
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains: DD-peptidase/beta-lactamase superfamily
Length: 330 amino acids
Theoretical weight: 35.41 KDa
Source organism: Neisseria gonorrhoeae FA6140
Expression system: Escherichia coli
UniProt:
- Canonical:
P08149 (Residues: 237-345, 346-574; Coverage: 56%)
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains: DD-peptidase/beta-lactamase superfamily
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 22-ID
Spacegroup:
P21
Expression system: Escherichia coli
