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Open data
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Basic information
Entry | Database: PDB / ID: 3n8l | ||||||
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Title | Crystal Structure of BlaC-E166A covalently bound with Ampicillin | ||||||
![]() | Beta-lactamase | ||||||
![]() | Hydrolase/Antibiotic / penicillin binding protein / beta-lactam covalent adduct / Hydrolase-Antibiotic complex | ||||||
Function / homology | ![]() : / : / beta-lactam antibiotic catabolic process / beta-lactamase activity / beta-lactamase / periplasmic space / response to antibiotic / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Tremblay, L.W. / Blanchard, J.S. | ||||||
![]() | ![]() Title: Structures of BlaC-E166A covalently bound to beta-lactams from all classes. Authors: Tremblay, L.W. / Blanchard, J.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 120.5 KB | Display | ![]() |
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PDB format | ![]() | 98.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 847.1 KB | Display | ![]() |
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Full document | ![]() | 849 KB | Display | |
Data in XML | ![]() | 15.1 KB | Display | |
Data in CIF | ![]() | 23.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 28214.689 Da / Num. of mol.: 1 / Mutation: E182A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P0C5C1, UniProt: P9WKD3*PLUS, beta-lactamase | ||||
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#2: Chemical | #3: Chemical | ChemComp-AIX / ( | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.25 Å3/Da / Density % sol: 45.28 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 0.1 M HEPES, 2 M NH4H2PO4, pH 7.5, Vapor diffusion, Sitting drop, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: 2009 |
Radiation | Monochromator: Si(111) Channel Cut / Protocol: SINGLE WAVELENGTH / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 1.4→40.1 Å / Num. obs: 50715 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.7 % / Biso Wilson estimate: 8.6 Å2 / Rmerge(I) obs: 0.086 / Net I/σ(I): 6 |
Reflection shell | Resolution: 1.4→1.436 Å / Redundancy: 7.8 % / Rmerge(I) obs: 0.356 / Mean I/σ(I) obs: 1.6 / Num. unique all: 7285 / % possible all: 99.35 |
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Processing
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Refinement | Method to determine structure: ![]() Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
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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 max: 64.64 Å2 / Biso mean: 10.194 Å2 / Biso min: 2.73 Å2
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Refinement step | Cycle: LAST / Resolution: 1.4→40.1 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.4→1.436 Å / Total num. of bins used: 20
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