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
CP5 (2z)-3-{[oxido(oxo)phosphino]oxy}-2-phenylacrylate
GOL Glycerol
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1SCW   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : TOWARD BETTER ANTIBIOTICS: CRYSTAL STRUCTURE OF R61 DD-PEPTIDASE INHIBITED BY A NOVEL MONOCYCLIC PHOSPHATE INHIBITOR
Release Data : 2004-06-22
Compound :
mol_id molecule chains synonym
1 D-alanyl-D-alanine carboxypeptidase A DD-peptidase, DD-carboxypeptidase
ec: 3.4.16.4
Source :
mol_id organism_scientific
1 Streptomyces sp.  (taxid:31952)
strain: R61
Authors : Silvaggi, N.R., Kaur, K., Adediran, S.A., Pratt, R.F., Kelly, J.A.
Keywords : CYCLIC PHOSPHATE, ANTIBIOTIC, PEPTIDOGLYCAN, PENICILLIN BINDING PROTEIN, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 1.13 Å )
Citation :

Toward Better Antibiotics: Crystallographic Studies of a Novel Class of DD-Peptidase/beta-Lactamase Inhibitors.

Silvaggi, N.R.,Kaur, K.,Adediran, S.A.  et al.
(2004)  Biochemistry  43 : 7046 - 7053

PubMed: 15170342
DOI: 10.1021/bi049612c

THE CRYSTAL STRUCTURE OF PHOSPHONATE-INHIBITED D-ALA-D-ALA PEPTIDASE REVEALS AN ANALOGUE OF A TETRAHEDRAL TRANSITION STATE

Silvaggi, N.R.,Anderson, J.W.,Brinsmade, S.R.  et al.
(2003)  Biochemistry  42 : 1199 - 1208

DOI: 10.1021/bi0268955

STRUCTURES OF TWO KINETIC INTERMEDIATES REVEAL SPECIES SPECIFICITY OF PENICILLIN-BINDING PROTEINS

McDonough, M.A.,Anderson, J.W.,Silvaggi, N.R.  et al.
(2002)  J.Mol.Biol.  322 : 111 - 122

DOI: 10.1016/S0022-2836(02)00742-8

THE REFINED CRYSTALLOGRAPHIC STRUCTURE OF A DD-PEPTIDASE PENICILLIN-TARGET ENZYME AT 1.6 A RESOLUTION

Kelly, J.A.,Kuzin, A.P.
(1995)  J.Mol.Biol.  254 : 223 - 236

DOI: 10.1006/jmbi.1995.0613

Chain : A
UniProt : P15555 (DAC_STRSR)
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 -
-