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- PDB-7keq: avibactam-CDD-1 6 minute complex -

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Basic information

Entry
Database: PDB / ID: 7keq
Titleavibactam-CDD-1 6 minute complex
ComponentsBeta-lactamase
KeywordsHYDROLASE/INHIBITOR / antibiotic resistance / mutant / Gram-positive / inhibitor / HYDROLASE / HYDROLASE-INHIBITOR complex
Function / homology
Function and homology information


penicillin binding / antibiotic catabolic process / beta-lactamase activity / beta-lactamase / response to antibiotic / membrane
Similarity search - Function
Beta-lactamase, class-D active site / Beta-lactamase class-D active site. / Penicillin-binding protein, transpeptidase / Penicillin binding protein transpeptidase domain / Beta-lactamase/transpeptidase-like
Similarity search - Domain/homology
Chem-FYG / Chem-NXL / Beta-lactamase
Similarity search - Component
Biological speciesClostridioides difficile (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2 Å
AuthorsSmith, C.A. / Vakulenko, S.B. / Stewart, N.K. / Toth, M.
CitationJournal: Acs Infect Dis. / Year: 2021
Title: Inhibition of the Clostridioides difficile Class D beta-Lactamase CDD-1 by Avibactam.
Authors: Stewart, N.K. / Toth, M. / Stasyuk, A. / Lee, M. / Smith, C.A. / Vakulenko, S.B.
History
DepositionOct 11, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 20, 2021Provider: repository / Type: Initial release
Revision 1.1May 26, 2021Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Beta-lactamase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,1749
Polymers36,0431
Non-polymers1,1318
Water2,774154
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1010 Å2
ΔGint-56 kcal/mol
Surface area11470 Å2
Unit cell
Length a, b, c (Å)123.536, 123.536, 123.536
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number212
Space group name H-MP4332
Components on special symmetry positions
IDModelComponents
11A-406-

SO4

21A-406-

SO4

31A-615-

HOH

41A-648-

HOH

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Components

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Protein , 1 types, 1 molecules A

#1: Protein Beta-lactamase / / CDD-1 beta-lactamase


Mass: 36043.055 Da / Num. of mol.: 1 / Mutation: K238A, K244A
Source method: isolated from a genetically manipulated source
Details: Class D beta-lactamase / Source: (gene. exp.) Clostridioides difficile (bacteria)
Gene: blaR1_4, blaR1_1, E5F39_11445, SAMEA2239407_03320, SAMEA3374989_01677
Production host: Escherichia coli (E. coli) / References: UniProt: A0A160YKM3, beta-lactamase

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Non-polymers , 5 types, 162 molecules

#2: Chemical ChemComp-NXL / (2S,5R)-1-formyl-5-[(sulfooxy)amino]piperidine-2-carboxamide / avibactam, bound form / NXL104, bound form / Avibactam


Mass: 267.260 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C7H13N3O6S / Feature type: SUBJECT OF INVESTIGATION / Comment: antibiotic, inhibitor*YM
#3: Chemical ChemComp-FYG / (2S,5R)-7-oxo-6-(sulfooxy)-1,6-diazabicyclo[3.2.1]octane-2-carboxamide / Avibactam / Avibactam


Mass: 265.244 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C7H11N3O6S / Comment: antibiotic, inhibitor*YM
#4: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: SO4
#5: Chemical ChemComp-MPD / (4S)-2-METHYL-2,4-PENTANEDIOL / 2-Methyl-2,4-pentanediol


Mass: 118.174 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H14O2 / Comment: precipitant*YM
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 154 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 2.18 Å3/Da / Density % sol: 43.56 %
Crystal growTemperature: 278 K / Method: vapor diffusion, sitting drop / Details: 0.1 M HEPES, pH 7.0, 2.4 M ammonium sulfate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL14-1 / Wavelength: 1.195 Å
DetectorType: RAYONIX MX-325 / Detector: CCD / Date: Jun 13, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.195 Å / Relative weight: 1
ReflectionResolution: 2→39.1 Å / Num. obs: 22396 / % possible obs: 99.9 % / Redundancy: 10.6 % / Biso Wilson estimate: 32.1 Å2 / CC1/2: 0.998 / Rpim(I) all: 0.044 / Rrim(I) all: 0.145 / Net I/σ(I): 13.2
Reflection shellResolution: 2→2.05 Å / Num. unique obs: 1615 / CC1/2: 0.718 / Rpim(I) all: 0.41

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Processing

Software
NameVersionClassification
PHENIXdev_3908refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
Aimlessdata scaling
REFMACphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS / Resolution: 2→39.07 Å / SU ML: 0.18 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 19.75 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2167 1112 4.98 %
Rwork0.1717 21239 -
obs0.1739 22351 99.95 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 87.02 Å2 / Biso mean: 31.5829 Å2 / Biso min: 16.91 Å2
Refinement stepCycle: final / Resolution: 2→39.07 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2005 0 81 157 2243
Biso mean--48.35 37.17 -
Num. residues----251
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0072172
X-RAY DIFFRACTIONf_angle_d1.1972950
X-RAY DIFFRACTIONf_dihedral_angle_d11.702327
X-RAY DIFFRACTIONf_chiral_restr0.062311
X-RAY DIFFRACTIONf_plane_restr0.006373
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 8 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all
2-2.090.24281300.20925882718
2.09-2.20.231270.191526082735
2.2-2.340.23051440.181825962740
2.34-2.520.24871380.183926222760
2.52-2.770.24581330.189626292762
2.77-3.170.22661400.184526572797
3.18-40.17481590.150826572816
4-39.070.22361410.160528823023

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