Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
SO4 Sulfate ion
MG Magnesium ion
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 3ZVW   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Unexpected tricovalent binding mode of boronic acids within the active site of a penicillin binding protein
Release Data : 2012-02-29
Compound :
mol_id molecule chains synonym
1 D-ALANYL-D-ALANINE CARBOXYPEPTIDASE A,B,C,D DD-CARBOXYPEPTIDASE, DD-PEPTIDASE, PENICILLIN-BINDING PROTEIN, PBP
ec: 3.4.16.4
Source :
mol_id organism_scientific
1 ACTINOMADURA SP. R39  (taxid:72570)
Authors : Sauvage, E., Zervosen, A., Herman, R., Kerff, F., Rocaboy, M., Charlier, P.
Keywords : HYDROLASE, PEPTIDOGLYCAN, PENICILLIN-BINDING, TETRAVALENT BORON
Exp. method : X-RAY DIFFRACTION ( 2.00 Å )
Citation :

Unexpected Tricovalent Binding Mode of Boronic Acids within the Active Site of a Penicillin- Binding Protein.

Zervosen, A.,Herman, R.,Kerff, F.  et al.
(2011)  J.Am.Chem.Soc.  133 : 10839

PubMed: 21574608
DOI: 10.1021/JA200696Y

Chain : A, B, C, D
UniProt : P39045 (DAC_ACTSP)
Reaction: EC: Evidence:
Physiological Direction:
Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine. 3.4.16.4 -
-