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- PDB-1ulp: N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI BETA-1... -

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Basic information

Entry
Database: PDB / ID: 1ulp
TitleN-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI BETA-1,4-GLUCANASE C, NMR, 25 STRUCTURES
ComponentsENDOGLUCANASE C
KeywordsCELLULOSE DEGRADATION / CELLULOSE-BINDING DOMAIN / HYDROLASE
Function / homology
Function and homology information


cellulase / cellulase activity / cellulose catabolic process
Similarity search - Function
Glycosyl hydrolases family 9 (GH9) active site signature 1. / Cellulase N-terminal ig-like domain / Cellulase, Ig-like domain / Glycoside hydrolase family 9, His active site / Glycosyl hydrolases family 9 (GH9) active site signature 2. / Glycosyl hydrolases family 9, Asp/Glu active sites / Glycosyl hydrolases family 9 (GH9) active site signature 3. / Carbohydrate-binding, CenC-like / Carbohydrate binding domain / Glycoside hydrolase family 9 ...Glycosyl hydrolases family 9 (GH9) active site signature 1. / Cellulase N-terminal ig-like domain / Cellulase, Ig-like domain / Glycoside hydrolase family 9, His active site / Glycosyl hydrolases family 9 (GH9) active site signature 2. / Glycosyl hydrolases family 9, Asp/Glu active sites / Glycosyl hydrolases family 9 (GH9) active site signature 3. / Carbohydrate-binding, CenC-like / Carbohydrate binding domain / Glycoside hydrolase family 9 / Glycosyl hydrolase family 9 / Six-hairpin glycosidase-like superfamily / Six-hairpin glycosidase superfamily / Galactose-binding domain-like / Immunoglobulin I-set / Immunoglobulin I-set domain / Galactose-binding-like domain superfamily / Immunoglobulin subtype / Immunoglobulin / Immunoglobulin E-set / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Jelly Rolls / Immunoglobulin-like fold / Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesCellulomonas fimi (bacteria)
MethodSOLUTION NMR / XPLOR V3.1
AuthorsJohnson, 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
DepositionJul 27, 1996Processing site: BNL
Revision 1.0Apr 1, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_nmr_software.name / _struct_ref_seq_dif.details
Revision 1.4Oct 23, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: ENDOGLUCANASE C


Theoretical massNumber of molelcules
Total (without water)15,4301
Polymers15,4301
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)25 / -
Representative

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Components

#1: Protein ENDOGLUCANASE C / CENC / ENDO-1 / 4-BETA-GLUCANASE C


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
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: SEE JOURNAL PUBLICATION

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Sample preparation

Sample conditionspH: 5.9 / Temperature: 308 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Varian UNITY / Manufacturer: Varian / Model: UNITY / Field strength: 500 MHz

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
NMRPipestructure solution
PIPPstructure solution
RefinementMethod: XPLOR V3.1 / Software ordinal: 1
NMR ensembleConformers submitted total number: 25

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