› 1oa4

X-ray diffraction
1.5Å resolution

Comparison of Family 12 Glycoside Hydrolases and Recruited Substitutions Important for Thermal Stability

Released:
DOI: 10.2210/pdb1oa4/pdb
PDB entry 1oa4 coloured by chain, front view.
PDB entry 1oa4 coloured by chain, side view.
PDB entry 1oa4 coloured by chain, top view.
Source organism: Streptomyces sp. 11AG8
Primary publication:
Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability.
Sandgren M, Gualfetti PJ, Shaw A, Gross LS, Saldajeno M, Day AG, Jones TA, Mitchinson C
Protein Sci 12 848-60 (2003)
PMID: 12649442

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191896 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CBM2 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 222 amino acids
Theoretical weight: 23.89 KDa
Source organism: Streptomyces sp. 11AG8
Expression system: Streptomyces lividans
UniProt:
  • Canonical: Q9KIH1 (Residues: 32-253; Coverage: 65%)
Gene name: cel12A
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 RU200
Spacegroup: P212121
Unit cell:
a: 65.16Å b: 54.63Å c: 62.59Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.181 0.193
Expression system: Streptomyces lividans

Quick links

Citations

6 review citations

Directed evolution of industrial enzymes: an update.
Cherry et al. (2003)
5 more

7 mentions without citation

Localizing frustration in native proteins and protein assemblies.
Ferreiro et al. (2007)
6 more