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Yorodumi- PDB-1hej: C-terminal xylan binding domain from Cellulomonas fimi xylanase 11A -
+Open data
-Basic information
Entry | Database: PDB / ID: 1hej | ||||||
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Title | C-terminal xylan binding domain from Cellulomonas fimi xylanase 11A | ||||||
Components | ENDO-1,4-BETA-XYLANASE D | ||||||
Keywords | HYDROLASE(XYLAN DEGRADATION) / HYDROLASE / XYLAN BINDING DOMAIN / XYLANASE / BETA-SHEET | ||||||
Function / homology | Function and homology information hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds / Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides / polysaccharide binding / endo-1,4-beta-xylanase activity / endo-1,4-beta-xylanase / xylan catabolic process Similarity search - Function | ||||||
Biological species | CELLULOMONAS FIMI (bacteria) | ||||||
Method | SOLUTION NMR / HYBRID DISTANCE GEOMETRY, SIMULATED ANNEALING | ||||||
Authors | Simpson, P.J. / Hefang, X. / Bolam, D.N. / White, P. / Hancock, S.M. / Gilbert, H.J. / Williamson, M.P. | ||||||
Citation | Journal: Biochemistry / Year: 2001 Title: Evidence for Synergy between Family 2B Carbohydrate Binding Modules in Cellulomonas Fimi Xylanase 11A Authors: Bolam, D.N. / Xie, H. / White, P. / Simpson, P.J. / Hancock, S.M. / Williamson, M.P. / Gilbert, H.J. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: AUTHOR PROVIDED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hej.cif.gz | 120.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hej.ent.gz | 99.2 KB | Display | PDB format |
PDBx/mmJSON format | 1hej.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/he/1hej ftp://data.pdbj.org/pub/pdb/validation_reports/he/1hej | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8750.339 Da / Num. of mol.: 1 / Fragment: XYLAN BINDING DOMAIN 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) CELLULOMONAS FIMI (bacteria) / Strain: JM83 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P54865, endo-1,4-beta-xylanase |
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Compound details | ENDOHYDROLYSIS OF 1,4-BETA-D-XYLOSIDIC LINKAGES IN XYLANS. BELONGS TO CELLULASE FAMILY G (FAMILY 11 ...ENDOHYDROL |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING HETERONUCLEAR NMR SPECTROSCOPY ON A UNIFORMLY 15N-LABELLED SAMPLE OF XBD2 |
-Sample preparation
Details | Contents: SODIUM PHOSPHATE 50 MM, SODIUM AZIDE 10 MM |
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Sample conditions | pH: 5 / Temperature: 303 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: HYBRID DISTANCE GEOMETRY, SIMULATED ANNEALING / Software ordinal: 1 / Details: YASAP PROTOCOL. DETAILS IN THE JRNL CITATION. | ||||||||||||
NMR ensemble | Conformer selection criteria: RANDOM SELECTION OF 5 FROM THE 23 LOWEST ENERGY STRUCTURES Conformers calculated total number: 50 / Conformers submitted total number: 5 |