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- PDB-9rqd: Fragment screening of FosAKP, cryo structure in complex with frag... -

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Basic information

Entry
Database: PDB / ID: 9rqd
TitleFragment screening of FosAKP, cryo structure in complex with fragment F2X-entry G03
ComponentsFosA family fosfomycin resistance glutathione transferase
KeywordsTRANSFERASE / antibiotic resistance / fosfomycin / fragment screening
Function / homology
Function and homology information


glutathione transferase / glutathione transferase activity / metal ion binding
Similarity search - Function
: / Glyoxalase/fosfomycin resistance/dioxygenase domain / Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily / Vicinal oxygen chelate (VOC) domain / Vicinal oxygen chelate (VOC) domain profile. / Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Similarity search - Domain/homology
: / 3-ethoxybenzene-1-carboximidamide / FosA family fosfomycin resistance glutathione transferase
Similarity search - Component
Biological speciesKlebsiella pneumoniae (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.17 Å
AuthorsGuenther, S. / Galchenkova, M. / Fischer, P. / Reinke, P.Y.A. / Falke, S. / Thekku Veedu, S. / Rodrigues, A.C. / Senst, J. / Meents, A.
Funding support Germany, 5items
OrganizationGrant numberCountry
German Federal Ministry for Education and Research16GW0277 Germany
German Federal Ministry for Education and Research13K22CHB Germany
Helmholtz AssociationFISCOV Germany
Helmholtz AssociationSFragX Germany
Helmholtz AssociationHIR3X Germany
CitationJournal: To Be Published
Title: Room temperature X-ray fragment screening with serial crystallography
Authors: Guenther, S. / Meents, A.
History
DepositionJun 25, 2025Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 15, 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: FosA family fosfomycin resistance glutathione transferase
B: FosA family fosfomycin resistance glutathione transferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)33,1978
Polymers32,6192
Non-polymers5786
Water8,215456
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6010 Å2
ΔGint-38 kcal/mol
Surface area12360 Å2
MethodPISA
Unit cell
Length a, b, c (Å)67.827, 89.773, 44.872
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212
Space group name HallP22ab
Symmetry operation#1: x,y,z
#2: x+1/2,-y+1/2,-z
#3: -x+1/2,y+1/2,-z
#4: -x,-y,z

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein FosA family fosfomycin resistance glutathione transferase / FosA_9_NZ_ACZD01000244 / Fosfomycin resistance protein FosA


Mass: 16309.347 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Klebsiella pneumoniae (bacteria)
Gene: fosA, BANRA_04523, DM078_10090, DW286_28140, E1814_00065, EAO17_17205, GJJ08_023570, GNF00_20975, H3G96_004055, JMZ77_23230, SAMEA3499874_02877, SAMEA3649591_01987, SAMEA3720909_04483
Production host: Escherichia coli (E. coli) / References: UniProt: A0A086IRG1, glutathione transferase

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Non-polymers , 5 types, 462 molecules

#2: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6O2
#3: Chemical ChemComp-RD4 / 3-ethoxybenzene-1-carboximidamide


Mass: 164.204 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C9H12N2O / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mn
#5: Chemical ChemComp-DMS / DIMETHYL SULFOXIDE


Mass: 78.133 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 456 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 2.09 Å3/Da / Density % sol: 41.26 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: The protein was crystallized by mixing 0.45 uL of 12 mg/mL protein solution in 10 mM Hepes, pH 7.5, 50 mM NaCl, with 0.45 uL 16% (w/v) PEG3350, 0.25 M MgCl2, 0.2 M KBr, 0.1 M BisTris, pH 5.5 ...Details: The protein was crystallized by mixing 0.45 uL of 12 mg/mL protein solution in 10 mM Hepes, pH 7.5, 50 mM NaCl, with 0.45 uL 16% (w/v) PEG3350, 0.25 M MgCl2, 0.2 M KBr, 0.1 M BisTris, pH 5.5 and 0.1 uL crystal microseeds in 26% (w/v) PEG3350, 0.25 M MgCl2, 0.2 M KBr, 0.1 M BisTris, pH 5.5. After at least 4 days of crystal growth, 40 nL of 100 mM compound, solubilized in 100% DMSO, was added using an acoustic droplet dispensing system.

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: PETRA III, DESY / Beamline: P11 / Wavelength: 1.0332 Å
DetectorType: DECTRIS EIGER2 X 16M / Detector: PIXEL / Date: Oct 7, 2023 / Details: KB mirrors
RadiationMonochromator: Si111 DCM / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0332 Å / Relative weight: 1
ReflectionResolution: 1.165→54.12 Å / Num. obs: 74426 / % possible obs: 78.9 % / Redundancy: 12 % / Biso Wilson estimate: 11.95 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.087 / Rpim(I) all: 0.026 / Rrim(I) all: 0.091 / Net I/σ(I): 14.2
Reflection shellResolution: 1.165→1.185 Å / Redundancy: 6.5 % / Rmerge(I) obs: 1.37 / Mean I/σ(I) obs: 1.1 / Num. unique obs: 2170 / CC1/2: 0.57 / Rpim(I) all: 0.57 / Rrim(I) all: 1.49 / % possible all: 47

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Processing

Software
NameVersionClassification
PHENIX1.21.2-5419_9999refinement
PHENIX1.21.2-5419_9999phasing
autoPROC1.0.5data processing
Coot0.9.8.92model building
XDSBUILT 20220820data reduction
Aimless0.7.4data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.17→54.12 Å / SU ML: 0.1074 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 16.9546
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.1706 3647 4.9 %
Rwork0.1434 70744 -
obs0.1447 74391 78.92 %
Solvent computationShrinkage radii: 0.6 Å / VDW probe radii: 0.9 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 16.04 Å2
Refinement stepCycle: LAST / Resolution: 1.17→54.12 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2144 0 34 456 2634
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00882438
X-RAY DIFFRACTIONf_angle_d1.12253339
X-RAY DIFFRACTIONf_chiral_restr0.0827345
X-RAY DIFFRACTIONf_plane_restr0.0115452
X-RAY DIFFRACTIONf_dihedral_angle_d16.094887
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.17-1.180.3075700.29271578X-RAY DIFFRACTION45.94
1.18-1.20.3117960.2581772X-RAY DIFFRACTION52.06
1.2-1.210.25611110.23161956X-RAY DIFFRACTION57.34
1.21-1.230.22911250.21522169X-RAY DIFFRACTION64.53
1.23-1.250.24431340.2092401X-RAY DIFFRACTION70.97
1.25-1.270.2505750.19911272X-RAY DIFFRACTION37.75
1.27-1.290.23561450.17283108X-RAY DIFFRACTION91.09
1.29-1.320.20441910.15493277X-RAY DIFFRACTION96.12
1.32-1.340.17491800.15053269X-RAY DIFFRACTION96.83
1.34-1.360.19671310.14992617X-RAY DIFFRACTION94.47
1.37-1.40.1751470.14452696X-RAY DIFFRACTION97.36
1.4-1.430.21181890.14363328X-RAY DIFFRACTION97.67
1.43-1.460.1801940.14521804X-RAY DIFFRACTION58.82
1.47-1.510.17661380.13632729X-RAY DIFFRACTION98.05
1.51-1.550.14591720.12253346X-RAY DIFFRACTION96.91
1.55-1.60.15761700.11333384X-RAY DIFFRACTION98.34
1.6-1.660.14691600.10923399X-RAY DIFFRACTION98.61
1.66-1.730.16871420.11792792X-RAY DIFFRACTION81.23
1.73-1.80.14631390.11793445X-RAY DIFFRACTION99.01
1.8-1.90.15721110.13462596X-RAY DIFFRACTION75.01
1.9-2.020.18691190.12812267X-RAY DIFFRACTION65.24
2.02-2.170.13561380.12652537X-RAY DIFFRACTION73.47
2.17-2.390.16341750.12793272X-RAY DIFFRACTION92.91
2.39-2.740.16781360.14232849X-RAY DIFFRACTION81.38
2.74-3.40.16641810.14523401X-RAY DIFFRACTION99.83
3.47-54.120.16331780.15843480X-RAY DIFFRACTION95.01

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