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PDBsum entry 3icg

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3icg
Jmol
Contents
Protein chains
452 a.a. *
Ligands
BTB ×4
EDO ×3
Waters ×1942
* Residue conservation analysis
Superseded by: 3ndy
PDB id:
3icg
Name: Hydrolase
Title: Crystal structure of the catalytic and carbohydrate binding endoglucanase d from clostridium cellulovorans
Structure: Endoglucanase d. Chain: a, b, c, d. Synonym: endo-1,4-beta-glucanase d, cellulase d. Engineered: yes
Source: Clostridium cellulovorans. Organism_taxid: 1493. Gene: engd, p28623. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.10Å     R-factor:   0.150     R-free:   0.195
Authors: C.M.Bianchetti,R.W.Smith,C.A.Bingman,G.N.Phillips Jr.
Key ref: C.M.Bianchetti et al. The structure of the catalytic and carbohydrate bindi domain of endoglucanase d from clostridium cellulovor. To be published, .
Date:
17-Jul-09     Release date:   28-Jul-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P28623  (GUND_CLOC7) -  Endoglucanase D
Seq:
Struc:
515 a.a.
452 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.4  - Cellulase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.