› 4hk8

X-ray diffraction
1.15Å resolution

Crystal Structures of Mutant Endo- -1,4-xylanase II Complexed with substrate (1.15 A) and Products (1.6 A)

Released:
DOI: 10.2210/pdb4hk8/pdb
PDB entry 4hk8 coloured by chain, front view.
PDB entry 4hk8 coloured by chain, side view.
PDB entry 4hk8 coloured by chain, top view.
Source organism: Trichoderma reesei
Primary publication:
X-ray crystallographic studies of family 11 xylanase Michaelis and product complexes: implications for the catalytic mechanism.
Wan Q, Zhang Q, Hamilton-Brehm S, Weiss K, Mustyakimov M, Coates L, Langan P, Graham D, Kovalevsky A
Acta Crystallogr D Biol Crystallogr 70 11-23 (2014)
PMID: 24419374

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153153 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Endo-1,4-beta-xylanase 2 Chain: A
Molecule details ›
Chain: A
Length: 189 amino acids
Theoretical weight: 20.73 KDa
Source organism: Trichoderma reesei
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P36217 (Residues: 35-223; Coverage: 93%)
Gene names: M419DRAFT_124931, xyn2
Sequence domains: Glycosyl hydrolases family 11
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: XYP
Carbohydrate polymer
2 bound ligands:
Ligand GOL 5 x GOL
Ligand CIT 1 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Unit cell:
a: 38.492Å b: 45.526Å c: 111.417Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.112 0.111 0.127
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Dissecting conformational contributions to glycosidase catalysis and inhibition.
Speciale et al. (2014)
1 more

13 mentions without citation

Endo-xylanases as tools for production of substituted xylooligosaccharides with prebiotic properties.
Nordberg Karlsson et al. (2018)
12 more