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- PDB-9eqe: X-ray crystal structure of LsAA9A -

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Basic information

Entry
Database: PDB / ID: 9eqe
TitleX-ray crystal structure of LsAA9A
ComponentsEndo-beta-1,4-glucanase D
KeywordsOXIDOREDUCTASE / LPMO
Function / homology
Function and homology information


lytic cellulose monooxygenase (C4-dehydrogenating) / cellulose catabolic process / monooxygenase activity / extracellular region / metal ion binding
Similarity search - Function
Auxiliary Activity family 9 / : / Auxiliary Activity family 9 (formerly GH61)
Similarity search - Domain/homology
CITRIC ACID / COPPER (II) ION / TRIETHYLENE GLYCOL / AA9 family lytic polysaccharide monooxygenase A
Similarity search - Component
Biological speciesPanus similis (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.7 Å
AuthorsFrandsen, K.E.H. / Di Domenico, V. / Lo Leggio, L.
Funding support Denmark, 5items
OrganizationGrant numberCountry
Novo Nordisk FoundationNNF17SA0027704 Denmark
Novo Nordisk FoundationNNF21OC0071799 Denmark
Danish Council for Independent Research8021-00273B Denmark
The Carlsberg FoundationCF16-0673 Denmark
The Carlsberg FoundationCF17-0533 Denmark
CitationJournal: To Be Published
Title: X-ray crystal structure of LsAA9A
Authors: Frandsen, K.E.H. / Di Domenico, V. / Lo Leggio, L.
History
DepositionMar 21, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 2, 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: Endo-beta-1,4-glucanase D
hetero molecules


Theoretical massNumber of molelcules
Total (without water)26,2717
Polymers25,2731
Non-polymers9986
Water2,288127
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)125.610, 125.610, 125.610
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number213
Space group name H-MP4132

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Components

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Protein / Sugars , 2 types, 3 molecules A

#1: Protein Endo-beta-1,4-glucanase D / Endoglucanase D / Carboxymethylcellulase D / Cellulase D


Mass: 25272.850 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Panus similis (fungus) / Production host: Aspergillus oryzae (mold) / References: UniProt: A0A0S2GKZ1, cellulase
#3: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 4 types, 131 molecules

#2: Chemical ChemComp-CU / COPPER (II) ION


Mass: 63.546 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: Cu / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical ChemComp-CIT / CITRIC ACID


Mass: 192.124 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H8O7 / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical ChemComp-PGE / TRIETHYLENE GLYCOL


Mass: 150.173 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H14O4
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 127 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Has protein modificationY

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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: 3.27 Å3/Da / Density % sol: 62.36 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop
Details: 3.5M NaCl, 0.1M citrate buffer pH 3.5 in 96-wells MRC-2 plates with 70 microliter of reservoirs and 0.3 microliter drops

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: PETRA III, DESY / Beamline: P11 / Wavelength: 1.805 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Aug 10, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.805 Å / Relative weight: 1
ReflectionResolution: 2.7→50 Å / Num. obs: 9557 / % possible obs: 97.5 % / Redundancy: 3.88 % / CC1/2: 0.994 / Rrim(I) all: 0.077 / Net I/σ(I): 15.52
Reflection shellResolution: 2.7→2.77 Å / Redundancy: 3.64 % / Num. unique obs: 683 / CC1/2: 0.973 / Rrim(I) all: 0.212 / % possible all: 97.3

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Processing

Software
NameVersionClassification
REFMAC5.8.0405refinement
XDSdata reduction
XSCALEdata scaling
REFMACphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS / Resolution: 2.7→44.45 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.894 / SU B: 10.873 / SU ML: 0.203 / Cross valid method: THROUGHOUT / ESU R: 0.704 / ESU R Free: 0.312 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.23848 508 5.3 %RANDOM
Rwork0.17632 ---
obs0.17966 9049 97.45 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 22.029 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å20 Å2
2--0 Å20 Å2
3---0 Å2
Refinement stepCycle: 1 / Resolution: 2.7→44.45 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1788 0 62 127 1977
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.0121954
X-RAY DIFFRACTIONr_bond_other_d0.0010.0161724
X-RAY DIFFRACTIONr_angle_refined_deg1.4041.6512700
X-RAY DIFFRACTIONr_angle_other_deg0.471.5653987
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.8785249
X-RAY DIFFRACTIONr_dihedral_angle_2_deg4.97957
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.97210247
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.0570.2301
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.022329
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02438
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_it1.5972.271963
X-RAY DIFFRACTIONr_mcbond_other1.5992.271963
X-RAY DIFFRACTIONr_mcangle_it2.6354.0881208
X-RAY DIFFRACTIONr_mcangle_other2.6384.091209
X-RAY DIFFRACTIONr_scbond_it2.2072.562991
X-RAY DIFFRACTIONr_scbond_other2.2122.57992
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other3.4894.6171488
X-RAY DIFFRACTIONr_long_range_B_refined5.7523.512147
X-RAY DIFFRACTIONr_long_range_B_other5.7323.582135
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.7→2.77 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.452 41 -
Rwork0.411 637 -
obs--97.84 %

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