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- PDB-3zcz: Crystal structure of a complex between Actinomadura R39 DD-peptid... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3zcz | ||||||
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Title | Crystal structure of a complex between Actinomadura R39 DD-peptidase and a trifluoroketone inhibitor | ||||||
![]() | D-ALANYL-D-ALANINE CARBOXYPEPTIDASE | ||||||
![]() | HYDROLASE / INHIBITOR / PEPTIDOGLYCAN | ||||||
Function / homology | ![]() serine-type D-Ala-D-Ala carboxypeptidase / serine-type D-Ala-D-Ala carboxypeptidase activity / peptidoglycan biosynthetic process / cell wall organization / regulation of cell shape / response to antibiotic / proteolysis / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Sauvage, E. / Herman, R. / Kerff, F. / Rocaboy, M. / Charlier, P. | ||||||
![]() | ![]() Title: Inhibition of Dd-Peptidases by a Specific Trifluoroketone: Crystal Structure of a Complex with the Actinomadura R39 Dd-Peptidase. Authors: Dzhekieva, L. / Adediran, S.A. / Herman, R. / Kerff, F. / Duez, C. / Charlier, P. / Sauvage, E. / Pratt, R.F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 678.5 KB | Display | ![]() |
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PDB format | ![]() | 572 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.4 MB | Display | ![]() |
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Full document | ![]() | 1.4 MB | Display | |
Data in XML | ![]() | 64.4 KB | Display | |
Data in CIF | ![]() | 88.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2xdmS 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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2 | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 47704.055 Da / Num. of mol.: 4 / Fragment: RESIDUES 50-516 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: P39045, serine-type D-Ala-D-Ala carboxypeptidase #2: Chemical | ChemComp-TFR / ( #3: Chemical | ChemComp-SO4 / #4: Chemical | ChemComp-MG / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 52.42 % / Description: NONE |
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Crystal grow | pH: 6.5 / Details: pH 6.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Date: Sep 23, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9801 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→48.9 Å / Num. obs: 61653 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 6.9 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 13.5 |
Reflection shell | Resolution: 2.6→2.74 Å / Redundancy: 6.9 % / Rmerge(I) obs: 0.63 / Mean I/σ(I) obs: 3.3 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2XDM Resolution: 2.6→47.9 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.927 / SU B: 25.69 / SU ML: 0.25 / Cross valid method: THROUGHOUT / ESU R: 1.115 / ESU R Free: 0.306 / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 61.38 Å2
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Refinement step | Cycle: LAST / Resolution: 2.6→47.9 Å
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Refine LS restraints |
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