PDBsum entry: 3b7m

Hydrolase

PDB id: 3b7m

Contents

Protein chains

216 a.a. *

Waters ×293

* Residue conservation analysis

PDB id:

3b7m

Name:

Hydrolase

Title:

Crystal structure of a meso-active thermo-stable cellulase (mt cel12a) derived by making non-contiguous mutations in the active surface of the cel12a cellulase of rhodothermus marinus

Structure:

Cellulase. Chain: a, b, c, d. Engineered: yes

Source:

Rhodothermus marinus. Organism_taxid: 29549. Gene: cela. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.10Å R-factor: 0.189 R-free: 0.238

Authors:

S.Karthikeyan,P.Guptasarma

Key ref:

D.Kapoor et al. Transplantation of the active surface of a mesophile cellulase onto the structural scaffold of a homologous thermophile cellulase through engineering of a surface beta sheet. To be published,

Date:

31-Oct-07 Release date: 27-Nov-07

Protein chains

O33897  (O33897_RHOMR) -  Cellulase

Seq: 260 a.a.

Struc: 216 a.a.*

* PDB and UniProt seqs differ at 50 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.2.1.4 - Cellulase.
• Reaction: Endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

 Gene Ontology (GO) functional annotation 

• Biological process: polysaccharide catabolic process (1 term)
• Biochemical function: hydrolase activity, hydrolyzing O-glycosyl compounds (2 terms)