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- PDB-9g5a: The structure of Aspergillus fumigatus UDP-GlcNAc pyrophosphoryla... -

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Basic information

Entry
Database: PDB / ID: 9g5a
TitleThe structure of Aspergillus fumigatus UDP-GlcNAc pyrophosphorylase in complex with a fragment
Components(UDP-N-acetylglucosamine diphosphorylase) x 2
KeywordsTRANSFERASE / Aspergillus / fragment / UAP
Function / homology
Function and homology information


UDP-N-acetylglucosamine diphosphorylase / UDP-N-acetylglucosamine diphosphorylase activity / UDP-N-acetylglucosamine biosynthetic process
Similarity search - Function
UDP-sugar pyrophosphorylase / UDPGP family / UTP--glucose-1-phosphate uridylyltransferase / Nucleotide-diphospho-sugar transferases
Similarity search - Domain/homology
: / Chem-GN1 / UDP-N-acetylglucosamine diphosphorylase
Similarity search - Component
Biological speciesAspergillus fumigatus (mold)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.87 Å
AuthorsYan, K.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom)MR/V001094/1 United Kingdom
CitationJournal: To Be Published
Title: Exploration of starting points for the chemical validation of UDP-N-acetylglucosamine pyrophosphorylase in Aspergillus fumigatus
Authors: Yan, K. / Stanley, M. / Raimi, O. / Kowalski, B. / Gurvic, D. / Grillenberger, S. / Chen, X. / Ferenbach, A.T. / Dorfmueller, H. / van Aalten, D.M.F.
History
DepositionJul 16, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 30, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
B: UDP-N-acetylglucosamine diphosphorylase
A: UDP-N-acetylglucosamine diphosphorylase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)108,5336
Polymers107,7032
Non-polymers8294
Water1,72996
1
B: UDP-N-acetylglucosamine diphosphorylase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)54,7095
Polymers53,8801
Non-polymers8294
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
A: UDP-N-acetylglucosamine diphosphorylase


Theoretical massNumber of molelcules
Total (without water)53,8231
Polymers53,8231
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)55.370, 137.500, 143.660
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein UDP-N-acetylglucosamine diphosphorylase


Mass: 53880.246 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Aspergillus fumigatus (mold) / Gene: KXV57_008857 / Production host: Escherichia coli (E. coli)
References: UniProt: A0A229XUD0, UDP-N-acetylglucosamine diphosphorylase
#2: Protein UDP-N-acetylglucosamine diphosphorylase


Mass: 53823.195 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Aspergillus fumigatus (mold) / Gene: KXV57_008857 / Production host: Escherichia coli (E. coli)
References: UniProt: A0A229XUD0, UDP-N-acetylglucosamine diphosphorylase
#3: Chemical ChemComp-A1IHU / 4-bromanyl-2-methyl-pyrazol-3-amine


Mass: 176.015 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C4H6BrN3 / Feature type: SUBJECT OF INVESTIGATION
#4: Sugar ChemComp-GN1 / 2-acetamido-2-deoxy-1-O-phosphono-alpha-D-glucopyranose / 2-(ACETYLAMINO)-2-DEOXY-1-O-PHOSPHONO-ALPHA-D-GLUCOPYRANOSE / N-ACETYL-D-GLUCOSAMINE-1-PHOSPHATE / N-acetyl-1-O-phosphono-alpha-D-glucosamine / 2-acetamido-2-deoxy-1-O-phosphono-alpha-D-glucose / 2-acetamido-2-deoxy-1-O-phosphono-D-glucose / 2-acetamido-2-deoxy-1-O-phosphono-glucose


Type: D-saccharide / Mass: 301.188 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C8H16NO9P
IdentifierTypeProgram
a-D-Glcp1PO3NAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 96 / Source method: isolated from a natural source / Formula: H2O
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: 2.54 Å3/Da / Density % sol: 51.55 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / Details: 0.2 M Sodium acetate 25 % PEG3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.98 Å
DetectorType: DECTRIS EIGER2 XE 16M / Detector: PIXEL / Date: Oct 9, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 1.87→51.36 Å / Num. obs: 91430 / % possible obs: 99.9 % / Redundancy: 13.2 % / CC1/2: 1 / Net I/σ(I): 16.7
Reflection shellResolution: 1.87→1.9 Å / Num. unique obs: 4481 / CC1/2: 0.389

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Processing

Software
NameVersionClassification
REFMAC5.8.0352refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.87→51.36 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.95 / SU B: 5.717 / SU ML: 0.154 / Cross valid method: THROUGHOUT / ESU R: 0.158 / ESU R Free: 0.146 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.25903 4580 5.1 %RANDOM
Rwork0.22633 ---
obs0.22807 85508 98.44 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 52.998 Å2
Baniso -1Baniso -2Baniso -3
1-2.87 Å2-0 Å2-0 Å2
2---2.77 Å2-0 Å2
3----0.1 Å2
Refinement stepCycle: 1 / Resolution: 1.87→51.36 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7268 0 43 96 7407
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0127477
X-RAY DIFFRACTIONr_bond_other_d0.0020.0166919
X-RAY DIFFRACTIONr_angle_refined_deg1.4821.65310107
X-RAY DIFFRACTIONr_angle_other_deg0.4911.56916169
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.9665932
X-RAY DIFFRACTIONr_dihedral_angle_2_deg7.76542
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.066101285
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.0680.21106
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.028462
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021429
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_it4.8485.4043734
X-RAY DIFFRACTIONr_mcbond_other4.8445.4043734
X-RAY DIFFRACTIONr_mcangle_it6.0648.0744655
X-RAY DIFFRACTIONr_mcangle_other6.0638.0754656
X-RAY DIFFRACTIONr_scbond_it5.1515.6553743
X-RAY DIFFRACTIONr_scbond_other5.1515.6563744
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other6.9428.3315450
X-RAY DIFFRACTIONr_long_range_B_refined8.69465.4037984
X-RAY DIFFRACTIONr_long_range_B_other8.69565.4077960
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.87→1.919 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.494 279 -
Rwork0.579 5120 -
obs--80.73 %

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