3b7m

X-ray diffraction
2.1Å resolution

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

Released:
Source organism: Rhodothermus marinus
Entry authors: Karthikeyan S, Guptasarma P

Function and Biology Details

Reaction catalysed:
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-128510 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cellulase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 216 amino acids
Theoretical weight: 23.77 KDa
Source organism: Rhodothermus marinus
Expression system: Escherichia coli
UniProt:
  • Canonical: O33897 (Residues: 38-195, 196-260; Coverage: 82%)
Gene name: celA
Sequence domains: Glycosyl hydrolase family 12
Structure domains: Jelly Rolls

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU ULTRAX 18
Spacegroup: P212121
Unit cell:
a: 60.398Å b: 111.874Å c: 133.707Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.186 0.238
Expression system: Escherichia coli