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Ligands
Code Name Style Show Link
BGC Beta-D-glucopyranose
: Polysaccharide
Non-standard Residues
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Glycosylation
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Code : 3NDZ   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose
Release Data : 2011-06-29
Compound :
mol_id molecule chains synonym
1 Endoglucanase D A,B,C,D Endo-1,4-beta-glucanase D, Cellulase D
ec: 3.2.1.4
fragment: UNP residues 32-376
mol_id molecule chains synonym
2 Endoglucanase D E,F,G,H Endo-1,4-beta-glucanase D, Cellulase D
ec: 3.2.1.4
fragment: UNP residues 409-515
Source :
mol_id organism_scientific expression_system
1 Clostridium cellulovorans  (taxid:1493) Escherichia coli  (taxid:562)
gene: engD
expression_system_strain: TOP10
expression_system_vector_type: plasmid
expression_system_plasmid: pBAD/thio-TOPO
mol_id organism_scientific expression_system
2 Clostridium cellulovorans  (taxid:1493) Escherichia coli  (taxid:562)
gene: engD
expression_system_strain: TOP10
expression_system_vector_type: plasmid
expression_system_plasmid: pBAD/thio-TOPO
Authors : Bianchetti, C.M., Smith, R.W., Bingman, C.A., Phillips Jr., G.N.
Keywords : cellotriose, endoglucanase, xylanase, carbohydrate binding domain, glucanase, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 2.08 Å )
Citation :

The structure of the catalytic and carbohydrate binding domain of endoglucanase D bound to cellotriose

Bianchetti, C.M.,Smith, R.W.,Bingman, C.A.  et al.
To be Published 

Chain : E, F, G, H
UniProt : P28623 (GUND_CLOC7)
Reaction: EC: Evidence:
Physiological Direction:
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. 3.2.1.4 -
-