› 1ojk

X-ray diffraction
1.5Å resolution

Anatomy of glycosynthesis: Structure and kinetics of the Humicola insolens Cel7BE197A and E197S glycosynthase mutants

Released:
DOI: 10.2210/pdb1ojk/pdb
PDB entry 1ojk coloured by chain, front view.
PDB entry 1ojk coloured by chain, side view.
PDB entry 1ojk coloured by chain, top view.
Source organism: Humicola insolens
Primary publication:
Anatomy of glycosynthesis: structure and kinetics of the Humicola insolens Cel7B E197A and E197S glycosynthase mutants.
Ducros VM, Tarling CA, Zechel DL, Brzozowski AM, Frandsen TP, von Ossowski I, Schülein M, Withers SG, Davies GJ
Chem Biol 10 619-28 (2003)
PMID: 12890535

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157519 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Endoglucanase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 402 amino acids
Theoretical weight: 44.57 KDa
Source organism: Humicola insolens
Expression system: Aspergillus oryzae
UniProt:
  • Canonical: P56680 (Residues: 1-402; Coverage: 100%)
Gene name: CEL7B
Sequence domains: Glycosyl hydrolase family 7
Structure domains: Glycoside hydrolase, family 7, domain

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, BGC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
2 bound ligands:
Ligand NAG 2 x NAG
Ligand GOL 2 x GOL
1 modified residue:
Ligand PCA 2 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 66.282Å b: 74.83Å c: 86.105Å
α: 90° β: 102.57° γ: 90°
R-values:
R R work R free
0.143 0.141 0.173
Expression system: Aspergillus oryzae

Quick links

Citations

7 review citations

Improving enzyme properties: when are closer mutations better?
Morley et al. (2005)
6 more

1 mention without citation

Glycosylated cyclophellitol-derived activity-based probes and inhibitors for cellulases.
de Boer et al. (2020)