› 4jjj

X-ray diffraction
1.6Å resolution

The structure of T. fusca GH48 D224N mutant

Released:
DOI: 10.2210/pdb4jjj/pdb
PDB entry 4jjj coloured by chain, front view.
PDB entry 4jjj coloured by chain, side view.
PDB entry 4jjj coloured by chain, top view.
Source organism: Thermobifida fusca
Primary publication:
Cel48A from Thermobifida fusca: structure and site directed mutagenesis of key residues.
Kostylev M, Alahuhta M, Chen M, Brunecky R, Himmel ME, Lunin VV, Brady J, Wilson DB
Biotechnol Bioeng 111 664-73 (2014)
PMID: 24264519

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175290 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
CBM2 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 642 amino acids
Theoretical weight: 71.76 KDa
Source organism: Thermobifida fusca
Expression system: Escherichia coli
UniProt:
  • Canonical: Q47NH7 (Residues: 343-984; Coverage: 68%)
Gene name: Tfu_1959
Sequence domains: Glycosyl hydrolase family 48
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: BGC, GLC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
6 bound ligands:
Ligand CA 4 x CA
Ligand NA 3 x NA
Ligand FE 4 x FE
Ligand ZN 21 x ZN
Ligand ACT 2 x ACT
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P21
Unit cell:
a: 56.458Å b: 88.494Å c: 66.753Å
α: 90° β: 113.72° γ: 90°
R-values:
R R work R free
0.124 0.121 0.164
Expression system: Escherichia coli

Quick links

Citations

13 citation in other articles

Kinetics of cellobiohydrolase (Cel7A) variants with lowered substrate affinity.
Kari et al. (2014)
12 more

2 mentions without citation

Natural diversity of glycoside hydrolase family 48 exoglucanases: insights from structure.
Brunecky et al. (2017)
1 more