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Open data
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Basic information
Entry | Database: PDB / ID: 5duj | ||||||
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Title | Crystal structure of ldtMt2 in complex with Faropenem adduct | ||||||
![]() | L,D-transpeptidase 2 | ||||||
![]() | TRANSFERASE / LD-TRANSPEPTIDASE / Peptidoglycan synthesis enzyme / cell wall enzyme | ||||||
Function / homology | ![]() peptidoglycan-based cell wall biogenesis / peptidoglycan-protein cross-linking / peptidoglycan metabolic process / peptidoglycan L,D-transpeptidase activity / Transferases; Acyltransferases; Aminoacyltransferases / acyltransferase activity / peptidoglycan-based cell wall / cell wall organization / regulation of cell shape / extracellular region ...peptidoglycan-based cell wall biogenesis / peptidoglycan-protein cross-linking / peptidoglycan metabolic process / peptidoglycan L,D-transpeptidase activity / Transferases; Acyltransferases; Aminoacyltransferases / acyltransferase activity / peptidoglycan-based cell wall / cell wall organization / regulation of cell shape / extracellular region / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Kumar, P. / Lamichhane, G. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Non-classical transpeptidases yield insight into new antibacterials. Authors: Kumar, P. / Kaushik, A. / Lloyd, E.P. / Li, S.G. / Mattoo, R. / Ammerman, N.C. / Bell, D.T. / Perryman, A.L. / Zandi, T.A. / Ekins, S. / Ginell, S.L. / Townsend, C.A. / Freundlich, J.S. / Lamichhane, G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 158.4 KB | Display | ![]() |
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PDB format | ![]() | 121.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 916.4 KB | Display | ![]() |
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Full document | ![]() | 922.8 KB | Display | |
Data in XML | ![]() | 31.6 KB | Display | |
Data in CIF | ![]() | 46.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5du7C ![]() 5dvpC ![]() 5dzjC ![]() 5dzpC ![]() 5e1gC ![]() 5e1iC ![]() 5e51C ![]() 5e5lC ![]() 5k69C ![]() 3vynS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 39532.004 Da / Num. of mol.: 2 / Fragment: residues 42-408 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: O53223, UniProt: I6Y9J2*PLUS, Transferases; Acyltransferases; Aminoacyltransferases #2: Chemical | ChemComp-SO4 / | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.87 Å3/Da / Density % sol: 57.12 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / Details: 20% 5000MME, 200mM ammonium sulfate / PH range: 7.0-8.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU SATURN 944+ / Detector: CCD / Date: Oct 7, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.17→50 Å / Num. obs: 42667 / % possible obs: 94.6 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.064 / Rsym value: 0.056 / Net I/av σ(I): 20.86 / Net I/σ(I): 20.86 |
Reflection shell | Resolution: 2.17→2.21 Å / Redundancy: 3 % / Rmerge(I) obs: 0.186 / Mean I/σ(I) obs: 4.19 / % possible all: 59.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3VYN Resolution: 2.17→50 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.914 / SU B: 5.402 / SU ML: 0.138 / Cross valid method: THROUGHOUT / ESU R: 0.234 / ESU R Free: 0.199 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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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: 27.029 Å2
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Refinement step | Cycle: 1 / Resolution: 2.17→50 Å
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Refine LS restraints |
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