Brand  (β version)

PDB ID: 3MZD

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Ligands
Code Name Style Show Link
CXV (2r,4s)-2-[(1s)-1-({[3-(2-chlorophenyl)-5-methyl-1,2-oxazol-4-yl]carbonyl}amino)-2-oxoethyl]-5,5-dimethyl-1,3-thiazolid ine-4-carboxylic acid PoSSuM
GOL Glycerol PoSSuM
Non-standard Residues
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Structure summary

Code : 3MZD   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/ANTIBIOTIC
Title : Structure of penicillin-binding protein 5 from E. coli: cloxacillin acyl-enzyme complex
Release Data : 2011-03-16
Compound :
mol_id molecule chains synonym
1 D-alanyl-D-alanine carboxypeptidase dacA A DD-carboxypeptidase, DD-peptidase, Beta-lactamase, Penicillin-binding protein 5, PBP-5
ec: 3.4.16.4, 3.5.2.6
fragment: Soluble construct
Source :
mol_id organism_scientific expression_system
1 Escherichia coli  (taxid:83333) Escherichia coli  (taxid:562)
strain: K12
gene: b0632, dacA, JW0627, pfv
expression_system_strain: MC1061
expression_system_vector_type: plasmid
expression_system_plasmid: PBR322
Authors : Nicola, G., Tomberg, J., Pratt, R.F., Nicholas, R.A., Davies, C.
Keywords : BETA-LACTAM ANTIBIOTIC, PENICILLIN-BINDING PROTEIN, DD-CARBOXYPEPTIDASE, HYDROLASE, HYDROLASE-ANTIBIOTIC complex
Exp. method : X-RAY DIFFRACTION ( 1.90 Å )
Citation :

Crystal structures of covalent complexes of beta-lactam antibiotics with Escherichia coli penicillin-binding protein 5: toward an understanding of antibiotic specificity

Nicola, G.,Tomberg, J.,Pratt, R.F.  et al.
(2010)  Biochemistry  49 : 8094 - 8104

PubMed: 20726582
DOI: 10.1021/bi100879m

Reaction

Chain : A
UniProt : P0AEB2 (DACA_ECOLI)
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 -
-
a beta-lactam + H2O = a substituted beta-amino acid 3.5.2.6 -
-