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- PDB-9fkl: The structure of glycosynthase IXT6 (E241G mutant), the intracell... -

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Basic information

Entry
Database: PDB / ID: 9fkl
TitleThe structure of glycosynthase IXT6 (E241G mutant), the intracellular xylanase of G.proteiniphilus T-6 in complex with xylobiose-F and xylohexaose-F molecules
ComponentsBeta-xylanase
KeywordsHYDROLASE / IXT6 / glycosynthase / Geobacillus proteiniphilus T-6 / Geobacillus stearothermophilus
Function / homology
Function and homology information


endo-1,4-beta-xylanase activity / endo-1,4-beta-xylanase / xylan catabolic process
Similarity search - Function
Glycosyl hydrolases family 10 (GH10) domain profile. / Glycoside hydrolase family 10 / Glycoside hydrolase family 10 domain / Glycosyl hydrolase family 10 / Glycosyl hydrolase family 10 / Glycoside hydrolase superfamily
Similarity search - Domain/homology
Biological speciesGeobacillus proteiniphilus (bacteria)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsHadad, N. / Chmelnik, O. / Dessau, M. / Shoham, Y. / Shoham, G.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: To Be Published
Title: The structure of glycosynthase IXT6 (E241G mutant), the intracellular xylanase of G.proteiniphilus T-6 in complex with xylobiose-F and xylohexaose-F molecules
Authors: Hadad, N. / Chmelnik, O. / Dessau, M. / Shoham, Y. / Shoham, G.
History
DepositionJun 3, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 18, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Beta-xylanase
B: Beta-xylanase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)78,3434
Polymers77,2462
Non-polymers1,0972
Water8,953497
1
A: Beta-xylanase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,4362
Polymers38,6231
Non-polymers8131
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Beta-xylanase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,9072
Polymers38,6231
Non-polymers2841
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)169.014, 80.526, 79.074
Angle α, β, γ (deg.)90.000, 91.993, 90.000
Int Tables number5
Space group name H-MC121
Space group name HallC2y
Symmetry operation#1: x,y,z
#2: -x,y,-z
#3: x+1/2,y+1/2,z
#4: -x+1/2,y+1/2,-z

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Components

#1: Protein Beta-xylanase


Mass: 38622.805 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Geobacillus proteiniphilus (bacteria) / Gene: xynA2 / Production host: Escherichia coli (E. coli) / References: UniProt: Q09LY9, endo-1,4-beta-xylanase
#2: Polysaccharide beta-D-xylopyranose-(1-4)-1-fluoro-D-xylopyranose


Type: oligosaccharide / Mass: 284.236 Da / Num. of mol.: 1 / Source method: obtained synthetically
DescriptorTypeProgram
[][<C5O3F1>]{[(1+1)][b-D-Xylp]{}}LINUCSPDB-CARE
#3: Polysaccharide beta-D-xylopyranose-(1-4)-beta-D-xylopyranose-(1-4)-beta-D-xylopyranose-(1-4)-beta-D-xylopyranose- ...beta-D-xylopyranose-(1-4)-beta-D-xylopyranose-(1-4)-beta-D-xylopyranose-(1-4)-beta-D-xylopyranose-(1-4)-beta-D-xylopyranose-(1-4)-1-fluoro-D-xylopyranose


Type: oligosaccharide / Mass: 812.695 Da / Num. of mol.: 1 / Source method: obtained synthetically
DescriptorTypeProgram
[][<C5O3F1>]{[(1+1)][b-D-Xylp]{[(4+1)][b-D-Xylp]{[(4+1)][b-D-Xylp]{[(4+1)][b-D-Xylp]{[(4+1)][b-D-Xylp]{}}}}}}LINUCSPDB-CARE
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 497 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationN

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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: 3.48 Å3/Da / Density % sol: 64.66 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 2M Sodium acetate and 0.1M Sodium cacodylate buffer at pH 6.5.

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.54 Å
DetectorType: DECTRIS PILATUS 200K / Detector: PIXEL / Date: Dec 10, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54 Å / Relative weight: 1
ReflectionResolution: 2.4→40.26 Å / Num. obs: 41609 / % possible obs: 100 % / Redundancy: 5 % / Biso Wilson estimate: 23.76 Å2 / CC1/2: 0.99 / Rmerge(I) obs: 0.1 / Rpim(I) all: 0.05 / Rrim(I) all: 0.1 / Net I/σ(I): 12.1
Reflection shellResolution: 2.4→2.48 Å / Rmerge(I) obs: 0.52 / Mean I/σ(I) obs: 2.4 / Num. unique obs: 4308 / CC1/2: 0.79 / Rpim(I) all: 0.31 / Rrim(I) all: 0.61

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Processing

Software
NameVersionClassification
PHENIX1.17.1_3660refinement
PHENIX1.17.1_3660refinement
XDSdata reduction
Aimlessdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.4→40.26 Å / SU ML: 0.2543 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 20.0917
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2057 2129 5.12 %
Rwork0.1532 39470 -
obs0.1558 41599 99.96 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 24.63 Å2
Refinement stepCycle: LAST / Resolution: 2.4→40.26 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5412 0 74 497 5983
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00715694
X-RAY DIFFRACTIONf_angle_d0.90737736
X-RAY DIFFRACTIONf_chiral_restr0.0563823
X-RAY DIFFRACTIONf_plane_restr0.0056998
X-RAY DIFFRACTIONf_dihedral_angle_d7.7647795
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4-2.460.28891500.20462605X-RAY DIFFRACTION99.96
2.46-2.520.30051430.2012593X-RAY DIFFRACTION100
2.52-2.590.25751300.19372631X-RAY DIFFRACTION99.96
2.59-2.660.27691390.19652588X-RAY DIFFRACTION100
2.66-2.750.27281670.18562620X-RAY DIFFRACTION99.96
2.75-2.850.24431420.17872599X-RAY DIFFRACTION99.96
2.85-2.960.25941490.18082624X-RAY DIFFRACTION100
2.96-3.090.25591390.17492629X-RAY DIFFRACTION99.96
3.09-3.260.21451340.16532640X-RAY DIFFRACTION100
3.26-3.460.18961200.152655X-RAY DIFFRACTION100
3.46-3.730.16181480.13022618X-RAY DIFFRACTION100
3.73-4.10.16081360.11712642X-RAY DIFFRACTION100
4.1-4.70.14821590.11192640X-RAY DIFFRACTION100
4.7-5.910.16931510.13282653X-RAY DIFFRACTION100
5.92-40.260.1931220.14962733X-RAY DIFFRACTION99.69

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