› 2w5f

X-ray diffraction
1.9Å resolution

High resolution crystallographic structure of the Clostridium thermocellum N-terminal endo-1,4-beta-D-xylanase 10B (Xyn10B) CBM22-1- GH10 modules complexed with xylohexaose

Released:
DOI: 10.2210/pdb2w5f/pdb
PDB entry 2w5f coloured by chain, front view.
PDB entry 2w5f coloured by chain, side view.
PDB entry 2w5f coloured by chain, top view.
Source organism: Acetivibrio thermocellus
Primary publication:
Putting an N-terminal end to the Clostridium thermocellum xylanase Xyn10B story: crystal structure of the CBM22-1-GH10 modules complexed with xylohexaose.
Najmudin S, Pinheiro BA, Prates JA, Gilbert HJ, Romão MJ, Fontes CM
J Struct Biol 172 353-62 (2010)
PMID: 20682344

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-156366 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Endo-1,4-beta-xylanase Y Chains: A, B
Molecule details ›
Chains: A, B
Length: 540 amino acids
Theoretical weight: 60.08 KDa
Source organism: Acetivibrio thermocellus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P51584 (Residues: 32-551; Coverage: 50%)
Gene name: xynY
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: XYP
Carbohydrate polymer
2 bound ligands:
Ligand ACT 9 x ACT
Ligand CD 13 x CD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P3221
Unit cell:
a: 173.178Å b: 173.178Å c: 131.71Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.166 0.164 0.194
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Enzymatic degradation of (ligno)cellulose.
Bornscheuer et al. (2014)
1 more

16 mentions without citation

An integrated suite of fast docking algorithms.
Mashiach et al. (2010)
15 more