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(-) Description

Title :  SOLUTION STRUCTURE, DYNAMICS AND BINDING STUDIES OF CTCBM11
 
Authors :  A. Viegas, E. J. Cabrita
Date :  11 Apr 12  (Deposition) - 06 Feb 13  (Release) - 24 Apr 13  (Revision)
Method :  SOLUTION NMR
Resolution :  NOT APPLICABLE
Chains :  NMR Structure  :  A  (20x)
NMR Structure *:  A  (1x)
Keywords :  Cellulosome, Hydrolase (Keyword Search: [Gene Ontology, PubMed, Web (Google))
 
Reference :  A. Viegas, J. Sardinha, F. Freire, D. F. Duarte, A. L. Carvalho, C. M. Fontes, M. J. Romao, A. L. Macedo, E. J. Cabrita
Solution Structure, Dynamics And Binding Studies Of A Famil 11 Carbohydrate-Binding Module From Clostridium Thermocellu (Ctcbm11).
Biochem. J. V. 451 289 2013
PubMed-ID: 23356867  |  Reference-DOI: 10.1042/BJ20120627

(-) Compounds

Molecule 1 - ENDOGLUCANASE H
    ChainsA
    EC Number3.2.1.4
    EngineeredYES
    Expression SystemESCHERICHIA COLI
    Expression System Taxid562
    Expression System VectorPET-21-A
    FragmentCBM11 DOMAIN RESIDUES 655-821
    GeneCELH, CTHE_1472
    Organism ScientificCLOSTRIDIUM THERMOCELLUM
    Organism Taxid203119
    StrainATCC 27405 / DSM 1237
    SynonymCELLULASE H, ENDO-1,4-BETA-GLUCANASE H, EGH

 Structural Features

(-) Chains, Units

  1
NMR Structure (20x)A
NMR Structure * (1x)A

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (1, 2)

NMR Structure (1, 2)
No.NameCountTypeFull Name
1CA2Ligand/IonCALCIUM ION
NMR Structure * (0, 0)
No.NameCountTypeFull Name
1CA-1Ligand/IonCALCIUM ION

(-) Sites  (2, 2)

NMR Structure (2, 2)
No.NameEvidenceResiduesDescription
1AC1SOFTWAREGLU A:91 , GLU A:101 , ASP A:135 , SER A:137 , THR A:139 , ASP A:141BINDING SITE FOR RESIDUE CA A 201
2AC2SOFTWAREASP A:12 , GLU A:14 , THR A:38 , ASN A:40 , ASP A:163BINDING SITE FOR RESIDUE CA A 202

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 2LRP)

(-) Cis Peptide Bonds  (1, 1)

NMR Structure
No.Residues
1Val A:16 -Leu A:17

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 2LRP)

(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 2LRP)

(-) Exons   (0, 0)

(no "Exon" information available for 2LRP)

(-) Sequences/Alignments

NMR Structure
   Reformat: Number of residues per line =  ('0' or empty: single-line sequence representation)
  Number of residues per labelling interval =   
  UniProt sequence: complete  aligned part    
   Show mapping: SCOP domains CATH domains Pfam domains Secondary structure (by author)
SAPs(SNPs) PROSITE motifs Exons
(details for a mapped element are shown in a popup box when the mouse pointer rests over it)
Chain A from PDB  Type:PROTEIN  Length:172
 aligned with GUNH_CLOTH | P16218 from UniProtKB/Swiss-Prot  Length:900

    Alignment length:172
                                   661       671       681       691       701       711       721       731       741       751       761       771       781       791       801       811       821  
           GUNH_CLOTH   652 VTPAVGEKMLDDFEGVLNWGSYSGEGAKVSTKIVSGKTGNGMEVSYTGTTDGYWGTVYSLPDGDWSKWLKISFDIKSVDGSANEIRFMIAEKSINGVGDGEHWVYSITPDSSWKTIEIPFSSFRRRLDYQPPGQDMSGTLDLDNIDSIHFMYANNKSGKFVVDNIKLIGATS 823
               SCOP domains d2lrpa_ A: automated matches                                                                                                                                                 SCOP domains
               CATH domains ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ......eeeee........eeeee...eeeeeeee....eeeeeeee.....eeeeeee..........eeeeeeee..........eeeee......eeeeee.........eeeeee.hhhee...................eeeee........eeeeeeeeeee.... Sec.struct. author
                 SAPs(SNPs) ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 2lrp A   1 MASAVGEKMLDDFEGVLNWGSYSGEGAKVSTKIVSGKTGNGMEVSYTGTTDGYWGTVYSLPDGDWSKWLKISFDIKSVDGSANEIRFMIAEKSINGVGDGEHWVYSITPDSSWKTIEIPFSSFRRRLDYQPPGQDMSGTLDLDNIDSIHFMYANNKSGKFVVDNIKLIGALE 172
                                    10        20        30        40        50        60        70        80        90       100       110       120       130       140       150       160       170  

   Legend:   → Mismatch (orange background)
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  x → Chemical Group (purple background, 'x', labelled with number + name, e.g. ACE or NH2)
  extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '|'

 Classification and Annotation

(-) SCOP Domains  (1, 1)

NMR Structure

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 2LRP)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 2LRP)

(-) Gene Ontology  (8, 8)

NMR Structure(hide GO term definitions)
Chain A   (GUNH_CLOTH | P16218)
molecular function
    GO:0008810    cellulase activity    Catalysis of the endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
    GO:0016787    hydrolase activity    Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3.
    GO:0016798    hydrolase activity, acting on glycosyl bonds    Catalysis of the hydrolysis of any glycosyl bond.
    GO:0004553    hydrolase activity, hydrolyzing O-glycosyl compounds    Catalysis of the hydrolysis of any O-glycosyl bond.
biological process
    GO:0005975    carbohydrate metabolic process    The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. Includes the formation of carbohydrate derivatives by the addition of a carbohydrate residue to another molecule.
    GO:0030245    cellulose catabolic process    The chemical reactions and pathways resulting in the breakdown of cellulose, a linear beta1-4 glucan of molecular mass 50-400 kDa with the pyranose units in the -4C1 conformation.
    GO:0008152    metabolic process    The chemical reactions and pathways, including anabolism and catabolism, by which living organisms transform chemical substances. Metabolic processes typically transform small molecules, but also include macromolecular processes such as DNA repair and replication, and protein synthesis and degradation.
    GO:0000272    polysaccharide catabolic process    The chemical reactions and pathways resulting in the breakdown of a polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.

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 Related Entries

(-) Entries Sharing at Least One Protein Chain (UniProt ID)

UniProtKB/Swiss-Prot
        GUNH_CLOTH | P162181v0a 2bv9 2bvd 2cip 2cit 2lro 2v3g 2vi0 4u3a 4u5i 4u5k 5byw

(-) Related Entries Specified in the PDB File

2lro