› 4xqw

X-ray diffraction
1.5Å resolution

X-ray structure analysis of xylanase-N44E with MES at pH6.0

Released:
DOI: 10.2210/pdb4xqw/pdb
PDB entry 4xqw coloured by chain, front view.
PDB entry 4xqw coloured by chain, side view.
PDB entry 4xqw coloured by chain, top view.
Source organism: Trichoderma reesei
Primary publication:
Direct determination of protonation states and visualization of hydrogen bonding in a glycoside hydrolase with neutron crystallography.
Wan Q, Parks JM, Hanson BL, Fisher SZ, Ostermann A, Schrader TE, Graham DE, Coates L, Langan P, Kovalevsky A
Proc Natl Acad Sci U S A 112 12384-9 (2015)
PMID: 26392527

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
Macromolecule:
Endo-1,4-beta-xylanase 2 Chain: A
Molecule details ›
Chain: A
Length: 189 amino acids
Theoretical weight: 20.74 KDa
Source organism: Trichoderma reesei
Expression system: Escherichia coli BL21
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

2 bound ligands:
Ligand IOD 5 x IOD
Ligand MES 1 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 47.99Å b: 59.627Å c: 69.552Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.174 0.179
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

The use of neutron scattering to determine the functional structure of glycoside hydrolase.
Nakamura et al. (2016)
15 other articles

1 mention without citation

Direct determination of protonation states and visualization of hydrogen bonding in a glycoside hydrolase with neutron crystallography.
Wan et al. (2015)