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- PDB-3cbh: THREE-DIMENSIONAL STRUCTURE OF CELLOBIOHYDROLASE FROM TRICHODERMA... -

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Basic information

Entry
Database: PDB / ID: 3cbh
TitleTHREE-DIMENSIONAL STRUCTURE OF CELLOBIOHYDROLASE FROM TRICHODERMA REESEI
ComponentsCELLOBIOHYDROLASE II CORE PROTEIN
KeywordsHYDROLASE (O-GLYCOSYL)
Function / homology
Function and homology information


cellulose 1,4-beta-cellobiosidase (non-reducing end) / cellulose 1,4-beta-cellobiosidase activity / cellulose binding / cellulose catabolic process / extracellular region / identical protein binding
Similarity search - Function
Glycosyl hydrolases family 6 signature 2. / Glycosyl hydrolases family 6 signature 1. / Glycoside hydrolase, family 6, conserved site / 1, 4-beta cellobiohydrolase / 1, 4-beta cellobiohydrolase superfamily / Glycosyl hydrolases family 6 / CBM1 (carbohydrate binding type-1) domain signature. / Cellulose-binding domain, fungal / Cellulose-binding domain superfamily / Fungal cellulose binding domain ...Glycosyl hydrolases family 6 signature 2. / Glycosyl hydrolases family 6 signature 1. / Glycoside hydrolase, family 6, conserved site / 1, 4-beta cellobiohydrolase / 1, 4-beta cellobiohydrolase superfamily / Glycosyl hydrolases family 6 / CBM1 (carbohydrate binding type-1) domain signature. / Cellulose-binding domain, fungal / Cellulose-binding domain superfamily / Fungal cellulose binding domain / CBM1 (carbohydrate binding type-1) domain profile. / Fungal-type cellulose-binding domain
Similarity search - Domain/homology
Biological speciesHypocrea jecorina (fungus)
MethodX-RAY DIFFRACTION / Resolution: 2 Å
AuthorsJones, T.A. / Rouvinen, J.
Citation
Journal: Science / Year: 1990
Title: Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei.
Authors: Rouvinen, J. / Bergfors, T. / Teeri, T. / Knowles, J.K. / Jones, T.A.
#1: Journal: J.Mol.Biol. / Year: 1989
Title: Crystallization of the Core Protein of Cellobiohydrolase II from Trichoderma Reesei
Authors: Bergfors, T. / Rouvinen, J. / Lehtovaara, P. / Caldentey, X. / Tomme, P. / Claeyssens, M. / Pettersson, G. / Teeri, T. / Knowles, J. / Jones, T.A.
History
DepositionAug 6, 1990Processing site: BNL
Revision 1.0Jan 15, 1991Provider: repository / Type: Initial release
Revision 1.1Mar 25, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 21, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: CELLOBIOHYDROLASE II CORE PROTEIN


Theoretical massNumber of molelcules
Total (without water)39,0551
Polymers39,0551
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)49.100, 75.800, 92.900
Angle α, β, γ (deg.)90.00, 103.20, 90.00
Int Tables number4
Space group name H-MP1211
Atom site foot note1: RESIDUES 358, 423, AND 444 ARE CIS PROLINES.

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Components

#1: Protein CELLOBIOHYDROLASE II CORE PROTEIN / Coordinate model: Cα atoms only


Mass: 39055.297 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Hypocrea jecorina (fungus)
References: UniProt: P07987, cellulose 1,4-beta-cellobiosidase (non-reducing end)

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 4.31 Å3/Da / Density % sol: 71.44 %
Crystal grow
*PLUS
pH: 6 / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
110 mg/mlprotein1drop
210 %PEG60001drop
320 mMMES1drop
420 %PEG60001reservoir
520 mMMES1reservoir

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Data collection

Reflection
*PLUS
Highest resolution: 0.55 Å / Lowest resolution: 2.8 Å / Num. obs: 32934 / % possible obs: 97 % / Num. measured all: 99337 / Rmerge(I) obs: 0.0764

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Processing

SoftwareName: X-PLOR / Classification: refinement
RefinementResolution: 2→8 Å / Rfactor Rwork: 0.155
Refinement stepCycle: LAST / Resolution: 2→8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms365 0 0 0 365
Refinement
*PLUS
Highest resolution: 2 Å / Lowest resolution: 8 Å / Rfactor all: 0.155
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.011
X-RAY DIFFRACTIONx_angle_deg2.7

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