› 3axe

X-ray diffraction
1.53Å resolution

The truncated Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase V18Y/W203Y in complex with cellotetraose (cellobiose density was observed)

Released:
DOI: 10.2210/pdb3axe/pdb
PDB entry 3axe coloured by chain, front view.
PDB entry 3axe coloured by chain, side view.
PDB entry 3axe coloured by chain, top view.
Source organism: Fibrobacter succinogenes subsp. succinogenes S85
Primary publication:
Rational design to improve thermostability and specific activity of the truncated Fibrobacter succinogenes 1,3-1,4-β-D-glucanase.
Huang JW, Cheng YS, Ko TP, Lin CY, Lai HL, Chen CC, Ma Y, Zheng Y, Huang CH, Zou P, Liu JR, Guo RT
Appl Microbiol Biotechnol 94 111-21 (2012)
PMID: 21959377

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148237 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Beta-glucanase Chain: A
Molecule details ›
Chain: A
Length: 249 amino acids
Theoretical weight: 27.83 KDa
Source organism: Fibrobacter succinogenes subsp. succinogenes S85
Expression system: Escherichia coli
UniProt:
  • Canonical: P17989 (Residues: 25-271; Coverage: 76%)
Gene names: FSU_0226, Fisuc_2961
Sequence domains: Glycosyl hydrolases family 16
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
2 bound ligands:
Ligand TRS 1 x TRS
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 40.091Å b: 70.404Å c: 76.589Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.182 0.201
Expression system: Escherichia coli

Quick links

Citations

2 review citations

From protein engineering to immobilization: promising strategies for the upgrade of industrial enzymes.
Singh et al. (2013)
1 more