2f6b

X-ray diffraction
2.8Å resolution

Structural and active site modification studies implicate Glu, Trp and Arg in the activity of xylanase from alkalophilic Bacillus sp. (NCL 87-6-10).

Released:
Source organism: Bacillus
Entry authors: Satyanarayana L, Balakrishnan H, Gaikward S, Suresh CG

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181966 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase Chains: A, B
Molecule details ›
Chains: A, B
Length: 206 amino acids
Theoretical weight: 22.95 KDa
Source organism: Bacillus
UniProt:
  • Canonical: Q7SIE3 (Residues: 2-206; Coverage: 99%)
Sequence domains: Glycosyl hydrolases family 11
Structure domains: Jelly Rolls

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 73.421Å b: 77.281Å c: 79.233Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.166 0.226