Function and Biology Details
Reaction catalysed:
Peptidyl-tRNA(1) + aminoacyl-tRNA(2) = tRNA(1) + peptidyl(aminoacyl-tRNA(2))
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
L,D-TPase catalytic domain-containing protein (preferred)
PDBe Complex ID:
PDB-CPX-174881 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L,D-TPase catalytic domain-containing protein
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 14.57 KDa
Source organism: Enterococcus faecium
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: L,D-transpeptidase catalytic domain
Structure domains: L,D-transpeptidase catalytic domain-like
Length: 129 amino acids
Theoretical weight: 14.57 KDa
Source organism: Enterococcus faecium
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q3Y185 (Residues: 341-466; Coverage: 27%)
Sequence domains: L,D-transpeptidase catalytic domain
Structure domains: L,D-transpeptidase catalytic domain-like
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
96%
Refinement method:
ARIA2.3
Expression system: Escherichia coli BL21(DE3)
