› 1tml

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF A THERMOPHILIC ENDOCELLULASE

Released:
DOI: 10.2210/pdb1tml/pdb
PDB entry 1tml coloured by chain, front view.
PDB entry 1tml coloured by chain, side view.
PDB entry 1tml coloured by chain, top view.
Source organism: Thermobifida fusca
Primary publication:
Crystal structure of the catalytic domain of a thermophilic endocellulase.
Spezio M, Wilson DB, Karplus PA
Biochemistry 32 9906-16 (1993)
PMID: 8399160

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-150674 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoglucanase E-2 Chain: A
Molecule details ›
Chain: A
Length: 286 amino acids
Theoretical weight: 30.44 KDa
Source organism: Thermobifida fusca
Expression system: Not provided
UniProt:
  • Canonical: P26222 (Residues: 32-317; Coverage: 70%)
Gene name: celB
Sequence domains: Glycosyl hydrolases family 6
Structure domains: 1, 4-beta cellobiohydrolase

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 43.35Å b: 65.94Å c: 43.41Å
α: 90° β: 107.69° γ: 90°
R-values:
R R work R free
0.184 0.184 not available
Expression system: Not provided

Quick links

Citations

13 review citations

Structures and mechanisms of glycosyl hydrolases.
Davies et al. (1995)
12 more

14 mentions without citation

Assessing sequence comparison methods with reliable structurally identified distant evolutionary relationships.
Brenner et al. (1998)
13 more