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Yorodumi- PDB-1ulp: N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI BETA-1... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ulp | ||||||
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Title | N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI BETA-1,4-GLUCANASE C, NMR, 25 STRUCTURES | ||||||
Components | ENDOGLUCANASE C | ||||||
Keywords | CELLULOSE DEGRADATION / CELLULOSE-BINDING DOMAIN / HYDROLASE | ||||||
Function / homology | Function and homology information cellular anatomical entity / cellulase / cellulase activity / cellulose catabolic process Similarity search - Function | ||||||
Biological species | Cellulomonas fimi (bacteria) | ||||||
Method | SOLUTION NMR / XPLOR V3.1 | ||||||
Authors | Johnson, P.E. / Mcintosh, L.P. | ||||||
Citation | Journal: Biochemistry / Year: 1996 Title: Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi CenC determined by nuclear magnetic resonance spectroscopy. Authors: Johnson, P.E. / Joshi, M.D. / Tomme, P. / Kilburn, D.G. / McIntosh, L.P. #1: Journal: Biochemistry / Year: 1996 Title: Interaction of Soluble Cellooligosaccharides with the N-Terminal Cellulose-Binding Domain of Cellulomonas Fimi Cenc. 2. NMR and Ultraviolet Absorption Spectroscopy Authors: Johnson, P.E. / Tomme, P. / Joshi, M.D. / Mcintosh, L.P. #2: Journal: Mol.Microbiol. / Year: 1992 Title: The Binding of Cellulomonas Fimi Endoglucanase C (Cenc) to Cellulose and Sephadex is Mediated by the N-Terminal Repeats Authors: Coutinho, J.B. / Gilkes, N.R. / Warren, R.A. / Kilburn, D.G. / Miller Junior, R.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ulp.cif.gz | 1017 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ulp.ent.gz | 876.4 KB | Display | PDB format |
PDBx/mmJSON format | 1ulp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ul/1ulp ftp://data.pdbj.org/pub/pdb/validation_reports/ul/1ulp | 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: 15429.660 Da / Num. of mol.: 1 / Fragment: N-TERMINAL CELLULOSE-BINDING DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Cellulomonas fimi (bacteria) / Plasmid: PTUG / Production host: Escherichia coli (E. coli) / Strain (production host): JM101 / References: UniProt: P14090, cellulase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: SEE JOURNAL PUBLICATION |
-Sample preparation
Sample conditions | pH: 5.9 / Temperature: 308 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian UNITY / Manufacturer: Varian / Model: UNITY / Field strength: 500 MHz |
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-Processing
Software |
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NMR software |
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Refinement | Method: XPLOR V3.1 / Software ordinal: 1 | ||||||||||||||||
NMR ensemble | Conformers submitted total number: 25 |