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Basic information

Entry
Database: PDB / ID: 4aek
TitleStructural and biochemical characterization of a novel Carbohydrate Binding Module of endoglucanase Cel5A from Eubacterium cellulosolvens
ComponentsENDOGLUCANASE CEL5A
KeywordsHYDROLASE / FAMILY 5 GLYCOSIDE HYDROLASE / CELLULOSOME
Function / homology
Function and homology information


glucan catabolic process / beta-glucosidase activity / cell surface / extracellular region
Similarity search - Function
Jelly Rolls - #1070 / Carbohydrate binding module 65 domain 1 / Carbohydrate binding module 65 domain 1 / Glycoside hydrolase, family 5 / Cellulase (glycosyl hydrolase family 5) / Glycoside hydrolase superfamily / Jelly Rolls / Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesEUBACTERIUM CELLULOSOLVENS (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.75 Å
AuthorsLuis, A.S. / Venditto, I. / Prates, J.A.M. / Ferreira, L.M.A. / Gilbert, H.J. / Fontes, C.M.G.A. / Najmudin, S.
Citation
Journal: J.Biol.Chem. / Year: 2013
Title: Understanding How Non-Catalytic Carbohydrate Binding Modules Can Display Specificity for Xyloglucan.
Authors: Luis, A.S. / Venditto, I. / Prates, J.A.M. / Ferrieira, L.M.A. / Temple, M.J. / Rogowski, A. / Basle, A. / Xue, J. / Knox, J.P. / Najmudin, S. / Fontes, C.M.G.A. / Gilbert, H.J.
#1: Journal: Acta Crystallogr.,Sect.F / Year: 2011
Title: Overproduction, Purification, Crystallization and Preliminary X-Ray Characterization of a Novel Carbohydrate-Binding Module of Endoglucanase Cel5A from Eubacterium Cellulosolvens.
Authors: Luis, A.S. / Alves, V.D. / Romao, M.J. / Prates, J.A.M. / Fontes, C.M.G.A. / Najmudin, S.
History
DepositionJan 11, 2012Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 16, 2013Provider: repository / Type: Initial release
Revision 1.1Feb 27, 2013Group: Database references
Revision 1.2May 8, 2019Group: Data collection / Derived calculations ...Data collection / Derived calculations / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc ...exptl_crystal_grow / pdbx_database_proc / pdbx_database_status / struct_conn
Item: _exptl_crystal_grow.temp / _pdbx_database_status.recvd_author_approval / _struct_conn.pdbx_leaving_atom_flag

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: ENDOGLUCANASE CEL5A


Theoretical massNumber of molelcules
Total (without water)14,8791
Polymers14,8791
Non-polymers00
Water1,65792
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)47.859, 47.859, 191.598
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number178
Space group name H-MP6122

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Components

#1: Protein ENDOGLUCANASE CEL5A


Mass: 14879.080 Da / Num. of mol.: 1 / Fragment: CARBOHYDRATE BINDING MODULE, RESIDUES 37-170
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) EUBACTERIUM CELLULOSOLVENS (bacteria) / Plasmid: PET28A / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q3LHN3
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 92 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.11 Å3/Da / Density % sol: 42 %
Description: MAD DATA WAS COLLECTED BUT STRUCTURE WAS SOLVED WITH SAD USING JUST THE PEAK DATA.
Crystal growTemperature: 292 K / pH: 4.6
Details: 0.23 M AMMONIUM SULFATE, 0.1 M SODIUM ACETATE PH 4.6, 26%(M/V) PEG 2K MME GROWN AT 292 K, USED 30% GLYCEROL AS CRYOPROTECTANT

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.9793, 0.97934, 0.9769
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 24, 2010
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
10.97931
20.979341
30.97691
ReflectionResolution: 1.75→63.87 Å / Num. obs: 13971 / % possible obs: 99.1 % / Redundancy: 5.5 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 10.4
Reflection shellResolution: 1.75→1.84 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.32 / Mean I/σ(I) obs: 1.7 / % possible all: 94.8

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Processing

Software
NameVersionClassification
REFMAC5.6.0117refinement
iMOSFLMdata reduction
SCALAdata scaling
SASAUTORICKSAWphasing
RefinementMethod to determine structure: SAD
Starting model: NONE

Resolution: 1.75→41.45 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.955 / SU B: 6.267 / SU ML: 0.096 / Cross valid method: THROUGHOUT / ESU R: 0.119 / ESU R Free: 0.117 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT. U VALUES WITH TLS ADDED. RESIDUES A37-38 AND A166-170 ARE DISORDERED. LYS A104 HAS DUAL ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT. U VALUES WITH TLS ADDED. RESIDUES A37-38 AND A166-170 ARE DISORDERED. LYS A104 HAS DUAL CONFORMATION. RESIDUES A56-59 ARE FLEXIBLE. LARGE BLOB NEAR SER A150. LYS A104 HAS DUAL CONFORMATION AND OTHER DISORDERED SIDE CHAINS WERE MODELED STEREOCHEMICALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.22712 691 5 %RANDOM
Rwork0.18826 ---
obs0.1902 13203 98.95 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 34.416 Å2
Baniso -1Baniso -2Baniso -3
1-1.32 Å20.66 Å20 Å2
2--1.32 Å20 Å2
3----1.98 Å2
Refinement stepCycle: LAST / Resolution: 1.75→41.45 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1003 0 0 92 1095
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.020.021042
X-RAY DIFFRACTIONr_bond_other_d0.0010.02965
X-RAY DIFFRACTIONr_angle_refined_deg2.0761.9451423
X-RAY DIFFRACTIONr_angle_other_deg0.91532203
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.6585128
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.982546
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.24315153
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.587151
X-RAY DIFFRACTIONr_chiral_restr0.1430.2151
X-RAY DIFFRACTIONr_gen_planes_refined0.010.0211177
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02236
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.75→1.795 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.297 33 -
Rwork0.285 732 -
obs--87.33 %
Refinement TLS params.Method: refined / Origin x: 17.2253 Å / Origin y: 29.6061 Å / Origin z: -0.0775 Å
111213212223313233
T0.2719 Å2-0.0028 Å2-0.0229 Å2-0.0643 Å20.0049 Å2--0.0153 Å2
L0.8963 °2-0.0672 °20.1797 °2-0.113 °2-0.186 °2--0.3945 °2
S-0.0503 Å °-0.0253 Å °0.0173 Å °-0.0587 Å °0.0562 Å °0.0051 Å °0.132 Å °-0.0334 Å °-0.0059 Å °
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A39 - 50
2X-RAY DIFFRACTION1A51 - 98
3X-RAY DIFFRACTION1A99 - 112
4X-RAY DIFFRACTION1A113 - 132
5X-RAY DIFFRACTION1A133 - 165

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