› 1gz1

X-ray diffraction
1.9Å resolution

Mutant D416A of the CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS in complex with methyl-cellobiosyl-4-deoxy-4-thio-beta-D-cellobioside

Released:
DOI: 10.2210/pdb1gz1/pdb
PDB entry 1gz1 coloured by chain, front view.
PDB entry 1gz1 coloured by chain, side view.
PDB entry 1gz1 coloured by chain, top view.
Source organism: Humicola insolens
Primary publication:
Structure of the Humicola insolens cellobiohydrolase Cel6A D416A mutant in complex with a non-hydrolysable substrate analogue, methyl cellobiosyl-4-thio-beta-cellobioside, at 1.9 A.
Varrot A, Frandsen TP, Driguez H, Davies GJ
Acta Crystallogr D Biol Crystallogr 58 2201-4 (2002)
PMID: 12454501

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-189902 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Exoglucanase-6A Chain: A
Molecule details ›
Chain: A
Length: 362 amino acids
Theoretical weight: 39.93 KDa
Source organism: Humicola insolens
Expression system: Aspergillus oryzae
UniProt:
  • Canonical: Q9C1S9 (Residues: 115-476; Coverage: 79%)
Gene names: avi2, cel6A
Sequence domains: Glycosyl hydrolases family 6
Structure domains: 1, 4-beta cellobiohydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: MGL, SGC, BGC
Ligand MGL 1 x MGL
Ligand SGC 1 x SGC
Ligand BGC 2 x BGC
2 bound ligands:
Ligand NAG 1 x NAG
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 48.257Å b: 68.38Å c: 55.18Å
α: 90° β: 112.39° γ: 90°
R-values:
R R work R free
0.168 0.166 0.211
Expression system: Aspergillus oryzae

Quick links

Citations

2 review citations

Glycoside hydrolases: catalytic base/nucleophile diversity.
Vuong et al. (2010)
1 more

1 mention without citation

Who's on base? Revealing the catalytic mechanism of inverting family 6 glycoside hydrolases.
Mayes et al. (2016)