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Ligands
Code Name Style Show Link
FER 3-(4-hydroxy-3-methoxyphenyl)-2-propenoic acid
Non-standard Residues
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Glycosylation
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Code : 1JT2   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : STRUCTURAL BASIS FOR THE SUBSTRATE SPECIFICITY OF THE FERUL DOMAIN OF THE CELLULOSOMAL XYLANASE Z FROM C. THERMOCELLUM
Release Data : 2002-03-27
Compound :
mol_id molecule chains synonym
1 PROTEIN (ENDO-1,4-BETA-XYLANASE Z) A FERULOYL ESTERASE, XYLANASE Z, 1,4-BETA-D-XYLAN XYLANOHYDROLASE Z
ec: 3.2.1.8
fragment: Residues 20-287
mutation: S172A
Source :
mol_id organism_scientific expression_system
1 Clostridium thermocellum  (taxid:1515) Escherichia coli BL21  (taxid:511693)
gene: XynZ
expression_system_strain: BL21
expression_system_vector_type: Plasmid
expression_system_plasmid: PET21B
Authors : Schubot, F.D., Kataeva, I.A., Blum, D.L., Shah, A.K., Ljungdahl, L.G., Rose, J.P., Wang, B.-C.
Keywords : FERULOYL ESTERASE, FERULIC ACID ESTERASE, FAE_XYNZ, XYNZ, FERULOYL ESTERASE Substrate complex, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 1.80 Å )
Citation :

Structural basis for the substrate specificity of the feruloyl esterase domain of the cellulosomal xylanase Z from Clostridium thermocellum.

Schubot, F.D.,Kataeva, I.A.,Blum, D.L.  et al.
(2001)  Biochemistry  40 : 12524 - 12532

PubMed: 11601976
DOI: 10.1021/bi011391c

Chain : A
UniProt : P10478 (XYNZ_ACET2)
Reaction: EC: Evidence:
Physiological Direction:
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. 3.2.1.8 -
-