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
BME Beta-mercaptoethanol
CL Chloride ion
RB Rubidium ion
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1SWY   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Use of a Halide Binding Site to Bypass the 1000-atom Limit to Ab initio Structure Determination
Release Data : 2004-11-23
Compound :
mol_id molecule chains synonym
1 Lysozyme A Lysis protein, Muramidase, Endolysin
ec: 3.2.1.17
mutation: D72A, R96E
Source :
mol_id organism_scientific expression_system
1 Enterobacteria phage T4  (taxid:10665) Escherichia coli  (taxid:562)
gene: E
expression_system_cell_line: RR1
expression_system_vector_type: plasmid
expression_system_plasmid: PH1403
Authors : Mooers, B.H.M., Matthews, B.W.
Keywords : Rb+ binding sites, Ab initio direct methods, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 1.06 Å )
Citation :

Use of an ion-binding site to bypass the 1000-atom limit to structure determination by direct methods.

Mooers, B.H.,Matthews, B.W.
(2004)  Acta Crystallogr.,Sect.D  60 : 1726 - 1737

PubMed: 15388918
DOI: 10.1107/S0907444904017020

Chain : A
UniProt : P00720 (ENLYS_BPT4)
Reaction: EC: Evidence:
Physiological Direction:
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. 3.2.1.17 HAMAP-Rule:MF_04110, PubMed:4865643
-