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
CED 5-methyl-2-[2-oxo-1-(2-thiophen-2-yl-acetylamino)-ethyl]-3,6-dihydro-2h-[1,3]thiazine-4-carboxylic acid
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 4N9K   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/ANTIBIOTIC
Title : crystal structure of beta-lactamse PenP_E166S in complex with cephaloridine
Release Data : 2014-09-10
Compound :
mol_id molecule chains synonym
1 Beta-lactamase B,A Penicillinase
ec: 3.5.2.6
fragment: Small exopenicillinase
mutation: E166S
Source :
mol_id organism_scientific expression_system
1 Bacillus licheniformis  (taxid:1402) Escherichia coli  (taxid:562)
gene: blaP, penP, penP blaP
expression_system_strain: BL21(DE3)
expression_system_vector_type: plasmid
expression_system_plasmid: pET30
Authors : Pan, X., Wong, W., Zhao, Y.
Keywords : hydrolase, HYDROLASE-ANTIBIOTIC complex
Exp. method : X-RAY DIFFRACTION ( 1.9300 Å )
Citation :

Perturbing the General Base Residue Glu166 in the Active Site of Class A beta-Lactamase Leads to Enhanced Carbapenem Binding and Acylation

Pan, X.,Wong, W.,He, Y.  et al.
(2014)  Biochemistry  53 : 5414 - 5423

PubMed: 25020031
DOI: 10.1021/bi401609h

Chain : B, A
UniProt : P00808 (BLAC_BACLI)
Reaction: EC: Evidence:
Physiological Direction:
a beta-lactam + H2O = a substituted beta-amino acid 3.5.2.6 PROSITE- ProRule:PRU10101
-