› 3vhn

X-ray diffraction
2.5Å resolution

Y61G mutant of Cellulase 12A from thermotoga maritima

Released:
DOI: 10.2210/pdb3vhn/pdb
PDB entry 3vhn coloured by chain, front view.
PDB entry 3vhn coloured by chain, side view.
PDB entry 3vhn coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Enhanced activity of Thermotoga maritima cellulase 12A by mutating a unique surface loop.
Cheng YS, Ko TP, Huang JW, Wu TH, Lin CY, Luo W, Li Q, Ma Y, Huang CH, Wang AH, Liu JR, Guo RT
Appl Microbiol Biotechnol 95 661-9 (2012)
PMID: 22170108

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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-562954 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Endo-1,4-beta-glucanase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 265 amino acids
Theoretical weight: 30.67 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q60032 (Residues: 1-257; Coverage: 100%)
Gene name: celA
Sequence domains: Glycosyl hydrolase family 12
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 91.91Å b: 124.039Å c: 127.556Å
α: 90° β: 107.06° γ: 90°
R-values:
R R work R free
0.189 0.185 0.245
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Defying the activity-stability trade-off in enzymes: taking advantage of entropy to enhance activity and thermostability.
Siddiqui KS. (2017)
3 more