› 4xpv

Hybrid

Neutron and X-ray structure analysis of xylanase: N44D at pH6

Released:
DOI: 10.2210/pdb4xpv/pdb
PDB entry 4xpv coloured by chain, front view.
PDB entry 4xpv coloured by chain, side view.
PDB entry 4xpv 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: 20.73 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 3 x IOD
Ligand DOD 173 x DOD
No modified residues

Experiments and Validation Details

Experimental Method: X-ray diffraction, Neutron Diffraction
X-ray source: RIGAKU MICROMAX-007 HF, LANSCE BEAMLINE PCS
Spacegroup: P212121
Unit cell:
a: 49.194Å b: 60.287Å c: 70.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.133 0.133 0.157
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)
14 other articles

4 mentions without citation

Fifteen years of the Protein Crystallography Station: the coming of age of macromolecular neutron crystallography.
Chen et al. (2017)
3 more