› 1ree

X-ray diffraction
1.6Å resolution

ENDO-1,4-BETA-XYLANASE II COMPLEX WITH 3,4-EPOXYBUTYL-BETA-D-XYLOSIDE

Released:
DOI: 10.2210/pdb1ree/pdb
PDB entry 1ree coloured by chain, front view.
PDB entry 1ree coloured by chain, side view.
PDB entry 1ree coloured by chain, top view.
Source organism: Trichoderma reesei
Primary publication:
Covalent binding of three epoxyalkyl xylosides to the active site of endo-1,4-xylanase II from Trichoderma reesei.
Havukainen R, Törrönen A, Laitinen T, Rouvinen J
Biochemistry 35 9617-24 (1996)
PMID: 8755744

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153153 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 190 amino acids
Theoretical weight: 20.84 KDa
Source organism: Trichoderma reesei
UniProt:
  • Canonical: P36217 (Residues: 34-223; Coverage: 93%)
Gene names: M419DRAFT_124931, xyn2
Sequence domains: Glycosyl hydrolases family 11
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand 07E 1 x 07E
Ligand BEZ 1 x BEZ
1 modified residue:
Ligand PCA 2 x PCA

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 81.84Å b: 60.81Å c: 38.09Å
α: 90° β: 94.2° γ: 90°
R-values:
R R work R free
0.181 0.181 0.223

Quick links

Citations

7 review citations

Structural and sequence-based classification of glycoside hydrolases.
Henrissat et al. (1997)
6 more