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PDBe Entry: 1xxn view

Crystal structure of a mesophilic xylanase A from Bacillus subtilis 1A1
Summary
Header hydrolasesearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.7 Å, R-factor: 17.344%, Free R-factor: 21.163%, Spacegroup: P 21 21 2
Released 18/10/2005, deposition: 07/11/2004, last revision: 22/09/2009
Authors Murakami, M.T.search; Ruller, R.search; Ward, R.J.search; Arni, R.K.search
Primary citation Correlation of temperature induced conformation change with optimum catalytic activity in the recombinant G/11 xylanase A from Bacillus subtilis strain 168 (1A1).
FEBS LETT.search vol:579, pag:6505-6510 (2005) [PubMed ID 16289057 ]search
Keywords family 11 xylanasesearch, thermostabilitysearch, hydrolasesearch
EC 3.2.1.8 ExPASy BRENDA search (A)
Organism Bacillus subtilis 1423search(A)
UniProt Endo-1,4-beta-xylanase A precursor (EC 3.2.1.8) (Xylanase A) (1,4-beta-D-xylan xylanohydrolase A) P18429search (A)
Solvent A
Polymers
Id Name Type UniProt Residues Observed
A Endo-1,4-beta-xylanase A Protein P18429 (XYNA_BACSU)search
185 100%
Heterogens
Id Name Ligands
A S,R MESO-TARTARIC ACID SRT search
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