CATH Domain 2y4aA02

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.50	3-Layer(bba) Sandwich
	3.50.80	D-tyrosyl-trna(Tyr) Deacylase; Chain: A;
	3.50.80.20	D-Ala-D-Ala carboxypeptidase C, peptidase S13

Domain Context

CATH Clusters

Superfamily	D-Ala-D-Ala carboxypeptidase C, peptidase S13
Functional Family

Enzyme Information

3.4.16.4

Serine-type D-Ala-D-Ala carboxypeptidase.

based on mapping to UniProt P39045

Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.

-!- A group of bacterial enzymes, membrane-bound. -!- Inhibited by beta-lactam antibiotics, which acylate the active site serine in the enzyme. -!- Distinct from EC 3.4.17.14. -!- Belongs to peptidase families S11, S12 and S13.

UniProtKB Entries (1)

P39045

DAC_ACTSP

Actinomadura sp. R39

D-alanyl-D-alanine carboxypeptidase

PDB Structure

PDB	2Y4A
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Unexpected Tricovalent Binding Mode of Boronic Acids within the Active Site of a Penicillin- Binding Protein. Zervosen, A., Herman, R., Kerff, F., Herman, A., Bouillez, A., Prati, F., Pratt, R.F., Frere, J.M., Joris, B., Luxen, A., Charlier, P., Sauvage, E. J.Am.Chem.Soc.