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Yorodumi- PDB-8veq: Crystal structure of transpeptidase domain of PBP2 from Neisseria... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8veq | ||||||
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Title | Crystal structure of transpeptidase domain of PBP2 from Neisseria gonorrhoeae cephalosporin-resistant strain H041 in complex with azlocillin | ||||||
Components | Probable peptidoglycan D,D-transpeptidase PenA | ||||||
Keywords | HYDROLASE / penicillin-binding protein / transpeptidase / complex | ||||||
Function / homology | Function and homology information peptidoglycan glycosyltransferase activity / serine-type D-Ala-D-Ala carboxypeptidase / FtsZ-dependent cytokinesis / serine-type D-Ala-D-Ala carboxypeptidase activity / division septum assembly / penicillin binding / peptidoglycan biosynthetic process / cell wall organization / regulation of cell shape / response to antibiotic ...peptidoglycan glycosyltransferase activity / serine-type D-Ala-D-Ala carboxypeptidase / FtsZ-dependent cytokinesis / serine-type D-Ala-D-Ala carboxypeptidase activity / division septum assembly / penicillin binding / peptidoglycan biosynthetic process / cell wall organization / regulation of cell shape / response to antibiotic / proteolysis / plasma membrane Similarity search - Function | ||||||
Biological species | Neisseria gonorrhoeae (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.4 Å | ||||||
Authors | Stratton, C. / Bala, S. / Davies, C. | ||||||
Funding support | United States, 1items
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Citation | Journal: Acs Infect Dis. / Year: 2024 Title: Ureidopenicillins Are Potent Inhibitors of Penicillin-Binding Protein 2 from Multidrug-Resistant Neisseria gonorrhoeae H041. Authors: Turner, J.M. / Stratton, C.M. / Bala, S. / Cardenas Alvarez, M. / Nicholas, R.A. / Davies, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8veq.cif.gz | 78.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8veq.ent.gz | 55.7 KB | Display | PDB format |
PDBx/mmJSON format | 8veq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8veq_validation.pdf.gz | 766.3 KB | Display | wwPDB validaton report |
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Full document | 8veq_full_validation.pdf.gz | 767.7 KB | Display | |
Data in XML | 8veq_validation.xml.gz | 13.9 KB | Display | |
Data in CIF | 8veq_validation.cif.gz | 18.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ve/8veq ftp://data.pdbj.org/pub/pdb/validation_reports/ve/8veq | HTTPS FTP |
-Related structure data
Related structure data | 8vbzC 8venC 8vepC C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 35361.496 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Azlocillin / Source: (gene. exp.) Neisseria gonorrhoeae (bacteria) / Strain: H041 / Gene: penA / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): K-12 References: UniProt: F2Z7K9, serine-type D-Ala-D-Ala carboxypeptidase |
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#2: Chemical | ChemComp-59H / ( |
#3: Water | ChemComp-HOH / |
Has ligand of interest | Y |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 45.5 % / Description: Plates |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 9.8 / Details: 32-40% PEG 600, 0.1 M CHES / PH range: 93-10.1 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 19, 2022 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→40.9 Å / Num. obs: 12832 / % possible obs: 92.6 % / Redundancy: 6.9 % / Biso Wilson estimate: 14.1 Å2 / CC1/2: 0.979 / CC star: 0.995 / Rmerge(I) obs: 0.182 / Rpim(I) all: 0.075 / Χ2: 0.878 / Net I/σ(I): 8.8 |
Reflection shell | Resolution: 2.4→2.44 Å / Rmerge(I) obs: 0.646 / Mean I/σ(I) obs: 2.1 / Num. unique obs: 669 / CC1/2: 0.797 / CC star: 0.942 / Rpim(I) all: 0.258 / Χ2: 0.475 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS / Resolution: 2.4→40.89 Å / Cor.coef. Fo:Fc: 0.883 / Cor.coef. Fo:Fc free: 0.888 / SU B: 10.254 / SU ML: 0.224 / Cross valid method: THROUGHOUT / ESU R: 0.603 / ESU R Free: 0.285 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 19.6 Å2
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Refinement step | Cycle: 1 / Resolution: 2.4→40.89 Å
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