PDBsum entry: 1h1n

Hydrolase

PDB id: 1h1n

Contents

Protein chains

305 a.a. *

Waters ×976

* Residue conservation analysis

PDB id:

1h1n

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: 3.2.1.4

Source:

Thermoascus aurantiacus. Organism_taxid: 5087. Strain: imi216529

Resolution:

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

Date:

19-Jul-02 Release date: 12-Aug-02

Protein chains

Q8TG26  (Q8TG26_THEAU) -  EGI

Seq: 335 a.a.

Struc: 305 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Biological process: carbohydrate metabolic process (1 term)
• Biochemical function: catalytic activity (3 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.

ABSTRACT

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.