› 1azh

Solution NMR

THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 14 STRUCTURES

Released:
DOI: 10.2210/pdb1azh/pdb
PDB entry 1azh coloured by chain, ensemble of 14 models, front view.
PDB entry 1azh coloured by chain, ensemble of 14 models, side view.
PDB entry 1azh coloured by chain, ensemble of 14 models, top view.
Source organism: Trichoderma reesei
Primary publication:
Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei.
Mattinen ML, Kontteli M, Kerovuo J, Linder M, Annila A, Lindeberg G, Reinikainen T, Drakenberg T
Protein Sci 6 294-303 (1997)
PMID: 9041630

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:
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
Macromolecule:
Exoglucanase 1 Chain: A
Molecule details ›
Chain: A
Length: 36 amino acids
Theoretical weight: 3.65 KDa
Source organism: Trichoderma reesei
Expression system: Not provided
UniProt:
  • Canonical: P62694 (Residues: 478-513; Coverage: 7%)
Gene name: cbh1
Sequence domains: Fungal cellulose binding domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Refinement method: distance geometry
Expression system: Not provided

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Citations

1 review citation

Advances in molecular engineering of carbohydrate-binding modules.
Armenta et al. (2017)
38 other articles