PDBsum entry 1h1n

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protein links
Hydrolase PDB id
Protein chains
305 a.a. *
Waters ×976
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Atomic resolution structure of the major endoglucanase from thermoascus aurantiacus
Structure: Endo type cellulase engi. Chain: a, b. Synonym: endo-1,4-glucanase. Ec:
Source: Thermoascus aurantiacus. Organism_taxid: 5087. Strain: imi216529
1.12Å     R-factor:   0.132     R-free:   0.171
Authors: F.Van Petegem,I.Vandenberghe,M.K.Bhat,J.Van Beeumen
Key ref: F.Van Petegem et al. (2002). Atomic resolution structure of the major endoglucanase from Thermoascus aurantiacus. Biochem Biophys Res Commun, 296, 161-166. PubMed id: 12147244 DOI: 10.1016/S0006-291X(02)00775-1
19-Jul-02     Release date:   12-Aug-02    
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Protein chains
Pfam   ArchSchema ?
Q8TG26  (Q8TG26_THEAU) -  EGI
335 a.a.
305 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.  - Cellulase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   2 terms 
  Biochemical function     hydrolase activity     4 terms  


DOI no: 10.1016/S0006-291X(02)00775-1 Biochem Biophys Res Commun 296:161-166 (2002)
PubMed id: 12147244  
Atomic resolution structure of the major endoglucanase from Thermoascus aurantiacus.
F.Van Petegem, I.Vandenberghe, M.K.Bhat, J.Van Beeumen.
The crystal structure of the major endoglucanase from the thermophilic fungus Thermoascus aurantiacus was determined by single isomorphous replacement at 1.12A resolution. The full sequence supports the classification of the protein in a subgroup of glycoside hydrolase family 5 for which no structural data are available yet. The active site shows eight critical residues, strictly conserved within family 5. In addition, aromatic residues that line the substrate-binding cleft and that are possibly involved in substrate-binding are identified. A number of residues seem to be conserved among members of the subtype, including a disulphide bridge between Cys212 and Cys249.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19458657 R.Berlemont, M.Delsaute, D.Pipers, S.D'Amico, G.Feller, M.Galleni, and P.Power (2009).
Insights into bacterial cellulose biosynthesis by functional metagenomics on Antarctic soil samples.
  ISME J, 3, 1070-1081.  
15857788 T.Wang, X.Liu, Q.Yu, X.Zhang, Y.Qu, P.Gao, and T.Wang (2005).
Directed evolution for engineering pH profile of endoglucanase III from Trichoderma reesei.
  Biomol Eng, 22, 89-94.  
15604820 L.Hildén, and G.Johansson (2004).
Recent developments on cellulases and carbohydrate-binding modules with cellulose affinity.
  Biotechnol Lett, 26, 1683-1693.  
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