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PDBe Entry: 1wb6 view

S954A MUTANT OF THE FERULOYL ESTERASE MODULE FROM CLOSTRIDIUM THERMOCELLUM COMPLEXED WITH VANILLATE
Summary
Header HYDROLASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.4 Å, R-factor: 11.8%, Free R-factor: 14.0%, Spacegroup: P 21 21 21
Released 24/05/2006, deposition: 30/10/2004, last revision: 24/02/2009
Authors Tarbouriech, N.search; Prates, J.A.search; Fontes, C.search; Davies, G.J.search
Primary citation Molecular Determinants of Substrate Specificity in the Feruloyl Esterase Module of Xylanase 10B from Clostridium Thermocellum
ACTA CRYSTALLOGR.,SECT.Dsearch vol:61, pag:194 (2005) [PubMed ID 15681871 ]search
Keywords ESTERASE FAMILY 1search, FERULIC ACIDsearch, GLYCOSIDASEsearch, HYDROLASEsearch, REPEATsearch, XYLAN DEGRADATIONsearch, XYLANASEsearch
EC 3.2.1.8 ExPASy BRENDA search (A B)
Organism Clostridium thermocellum 1515search(A B)
UniProt Endo-1,4-beta-xylanase Y precursor (EC 3.2.1.8) (Xylanase Y) (1,4-beta-D-xylan xylanohydrolase Y) (XylY) P51584search (A B)
Solvent A, B
Related entries 1dyo, 1gkk, 1gkl, 1h6x, 1h6y, 1ohz, 1wb4, 1wb5, 2ccl
Polymers
Id Name Type UniProt Residues Observed
A, B ENDO-1,4-BETA-XYLANASE Y Protein P51584 (XYNY_CLOTM)search
297 95%
Heterogens
Id Name Ligands
A, B VANILLATE VXX search
A, B GLYCEROL GOL search
A, B ACETATE ION ACT search
A, B CADMIUM ION CD search
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