› 5jrm

X-ray diffraction
1.56Å resolution

Crystal Structure of a Xylanase at 1.56 Angstroem resolution

Released:
DOI: 10.2210/pdb5jrm/pdb
PDB entry 5jrm coloured by chain, front view.
PDB entry 5jrm coloured by chain, side view.
PDB entry 5jrm coloured by chain, top view.
Source organism: Fusarium oxysporum
Primary publication:
Structural and functional characterization of a highly stable endo-β-1,4-xylanase from Fusarium oxysporum and its development as an efficient immobilized biocatalyst.
Gómez S, Payne AM, Savko M, Fox GC, Shepard WE, Fernandez FJ, Cristina Vega M
Biotechnol Biofuels 9 191 (2016)
PMID: 27602054

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-197835 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase Chain: A
Molecule details ›
Chain: A
Length: 194 amino acids
Theoretical weight: 21.25 KDa
Source organism: Fusarium oxysporum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: X0M5X0 (Residues: 42-232; Coverage: 90%)
Gene name: FOTG_15646
Sequence domains: Glycosyl hydrolases family 11
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand GOL 1 x GOL
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 2
Spacegroup: P21212
Unit cell:
a: 105.233Å b: 35.886Å c: 48.343Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.187 0.234
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Cultivation of Mushrooms and Their Lignocellulolytic Enzyme Production Through the Utilization of Agro-Industrial Waste.
Kumla et al. (2020)
2 more