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
CA Calcium ion
CL Chloride ion
MG Magnesium ion
PEG Di(hydroxyethyl)ether
GLC Alpha-D-glucopyranose
: Polysaccharide
Non-standard Residues
Code Name Show
MSE Selenomethionine
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 5HPO   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Cycloalternan-forming enzyme from Listeria monocytogenes in complex with maltopentaose
Release Data : 2017-01-25
Compound :
mol_id molecule chains
1 Lmo2446 protein A
Source :
mol_id organism_scientific expression_system
1 Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)  (taxid:169963) Escherichia coli  (taxid:511693)
strain: ATCC BAA-679 / EGD-e
gene: lmo2446
expression_system_strain: BL21 Magic
expression_system_vector_type: plasmid
expression_system_plasmid: pMCSG7
Authors : Halavaty, A.S., Light, S.H., Minasov, G., Winsor, J., Grimshaw, S., Shuvalova, L., Peterson, S., Anderson, W.F., Center for Structural Genomics of Infectious Diseases (CSGID)
Keywords : lmo2446, Listeria monocytogenes EGD-e, Center for Structural Genomics of Infectious Diseases, CSGID, SUGAR BINDING PROTEIN, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 1.80 Å )
Citation :

Transferase Versus Hydrolase: The Role of Conformational Flexibility in Reaction Specificity.

Light, S.H.,Cahoon, L.A.,Mahasenan, K.V.  et al.
(2017)  Structure  25 : 295 - 304

PubMed: 28089449
DOI: 10.1016/j.str.2016.12.007

Chain : A
UniProt : Q8Y4J2 (Q8Y4J2_LISMO)
Reaction : -