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- PDB-1e8p: Characterisation of the cellulose docking domain from Piromyces equi -

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Basic information

Entry
Database: PDB / ID: 1e8p
TitleCharacterisation of the cellulose docking domain from Piromyces equi
ComponentsEndoglucanase 45A
KeywordsCELLULOSE DOCKING DOMAIN / CELLULASE
Function / homology
Function and homology information


cellulase / cellulase activity / cellulose catabolic process
Similarity search - Function
Endoglucanase; Chain: A / Cellulose docking domain, dockering / Glycoside hydrolase, family 45 / Glycosyl hydrolase family 45 / Glycosyl hydrolases family 45 active site. / Fungal dockerin domain superfamily / Cellulose or protein binding domain / CBM10/dockerin domain / CBM10 (carbohydrate-binding type-10) domain profile. / RlpA-like domain superfamily ...Endoglucanase; Chain: A / Cellulose docking domain, dockering / Glycoside hydrolase, family 45 / Glycosyl hydrolase family 45 / Glycosyl hydrolases family 45 active site. / Fungal dockerin domain superfamily / Cellulose or protein binding domain / CBM10/dockerin domain / CBM10 (carbohydrate-binding type-10) domain profile. / RlpA-like domain superfamily / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
Biological speciesPiromyces equi (fungus)
MethodSOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING
Model type detailsMINIMIZED AVERAGE
AuthorsRaghothama, S. / Eberhardt, R.Y. / White, P. / Hazlewood, G.P. / Gilbert, H.J. / Simpson, P.J. / Williamson, M.P.
CitationJournal: Nat. Struct. Biol. / Year: 2001
Title: Characterization of a cellulosome dockerin domain from the anaerobic fungus Piromyces equi.
Authors: Raghothama, S. / Eberhardt, R.Y. / Simpson, P. / Wigelsworth, D. / White, P. / Hazlewood, G.P. / Nagy, T. / Gilbert, H.J. / Williamson, M.P.
History
DepositionSep 28, 2000Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 7, 2001Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jun 20, 2018Group: Data collection / Database references ...Data collection / Database references / Source and taxonomy / Structure summary
Category: citation / citation_author ...citation / citation_author / entity / entity_src_gen / struct_ref / struct_ref_seq / struct_ref_seq_dif
Item: _citation.journal_abbrev / _citation.page_last ..._citation.journal_abbrev / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _citation_author.name / _entity.pdbx_description / _entity_src_gen.pdbx_beg_seq_num / _entity_src_gen.pdbx_end_seq_num / _entity_src_gen.pdbx_gene_src_gene / _entity_src_gen.pdbx_gene_src_scientific_name / _entity_src_gen.pdbx_seq_type / _struct_ref.db_code / _struct_ref.pdbx_align_begin / _struct_ref.pdbx_db_accession / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.pdbx_db_accession / _struct_ref_seq_dif.pdbx_seq_db_accession_code

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Endoglucanase 45A


Theoretical massNumber of molelcules
Total (without water)5,0441
Polymers5,0441
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / 50MINIMISED AVERAGE STRUCTURE
Representative

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Components

#1: Protein/peptide Endoglucanase 45A / DOCKERIN


Mass: 5044.316 Da / Num. of mol.: 1 / Fragment: CELLULOSE DOCKING DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Piromyces equi (fungus) / Gene: cel45A / Plasmid: PGEX / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q9P868
Sequence detailsSER 2, NMR SAMPLE HAS SER AT THIS POSITION

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D - HSQC/NOESY
121HNHA
131HNHB
1412D - HSQC
15115N DECOUPLED TOCSY
161NOESY
171DQF-COSY
181E.COSY
NMR detailsText: MINIMISED AVERAGE STRUCTURE. THE STRUCTURE WAS DETERMINED USING STANDARD 2D & 3D NMR TECHNIQUES.

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Sample preparation

DetailsContents: 50 MM SODIUM PHOSPHATE
Sample conditionspH: 6.5 / Pressure: AMBIENT / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX5001
Bruker DRXBrukerDRX6002

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
FELIXstructure solution
RefinementMethod: DISTANCE GEOMETRY, SIMULATED ANNEALING / Software ordinal: 1 / Details: YASAP PROTOCOL
NMR ensembleConformer selection criteria: MINIMISED AVERAGE STRUCTURE / Conformers calculated total number: 50 / Conformers submitted total number: 1

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