› 5cel

X-ray diffraction
1.9Å resolution

CBH1 (E212Q) CELLOTETRAOSE COMPLEX

Released:
DOI: 10.2210/pdb5cel/pdb
PDB entry 5cel coloured by chain, front view.
PDB entry 5cel coloured by chain, side view.
PDB entry 5cel coloured by chain, top view.
Source organism: Trichoderma reesei
Primary publication:
High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei.
Divne C, Ståhlberg J, Teeri TT, Jones TA
J Mol Biol 275 309-25 (1998)
PMID: 9466911

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains
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-158661 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Exoglucanase 1 Chain: A
Molecule details ›
Chain: A
Length: 434 amino acids
Theoretical weight: 46.07 KDa
Source organism: Trichoderma reesei
Expression system: Trichoderma reesei
UniProt:
  • Canonical: P62694 (Residues: 18-451; Coverage: 88%)
Gene name: cbh1
Sequence domains: Glycosyl hydrolase family 7
Structure domains: Glycoside hydrolase, family 7, domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: I222
Unit cell:
a: 83.05Å b: 82.95Å c: 110.85Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.24
Expression system: Trichoderma reesei

Quick links

Citations

28 review citations

Hyaluronidases: their genomics, structures, and mechanisms of action.
Stern et al. (2006)
27 more

4 mentions without citation

Assessment of risk conferred by coding and regulatory variations of TMPRSS2 and CD26 in susceptibility to SARS-CoV-2 infection in human.
Senapati et al. (2020)
3 more