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Open data
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Basic information
Entry | Database: PDB / ID: 1dja | ||||||
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Title | STRUCTURE OF BETA-LACTAMASE PRECURSOR, K73H MUTANT, AT 298K | ||||||
![]() | BETA-LACTAMASE | ||||||
![]() | HYDROLASE / ANTIBIOTIC RESISTANCE / PLASMID / TRANSPOSABLE ELEMENT | ||||||
Function / homology | ![]() beta-lactam antibiotic catabolic process / beta-lactamase activity / beta-lactamase / response to antibiotic Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Chen, C.C.H. / Herzberg, O. | ||||||
![]() | ![]() Title: Structure and kinetics of the beta-lactamase mutants S70A and K73H from Staphylococcus aureus PC1. Authors: Chen, C.C. / Smith, T.J. / Kapadia, G. / Wasch, S. / Zawadzke, L.E. / Coulson, A. / Herzberg, O. #1: ![]() Title: An Engineered Staphylococcus Aureus Pc1 Beta-Lactamase that Hydrolyses Third-Generation Cephalosporins Authors: Zawadzke, L.E. / Smith, T.J. / Herzberg, O. #2: ![]() Title: Refined Crystal Structure of Beta-Lactamase from Staphylococcus Aureus Pc1 at 2.0 Authors: Herzberg, O. #3: ![]() Title: Bacterial Resistance to Beta-Lactam Antibiotics. Crystal Structure of Beta-Lactamase from Staphylococcus Aureus Pc1 at 2.5 A Resolution Authors: Herzberg, O. / Moult, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 65.9 KB | Display | ![]() |
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PDB format | ![]() | 47.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 365.9 KB | Display | ![]() |
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Full document | ![]() | 368.8 KB | Display | |
Data in XML | ![]() | 6.5 KB | Display | |
Data in CIF | ![]() | 10.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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 on special symmetry positions |
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Components
#1: Protein | Mass: 28983.375 Da / Num. of mol.: 1 / Mutation: A30M, K73H Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.03 Å3/Da / Density % sol: 65 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 8 / Method: vapor diffusion, hanging dropDetails: drop consists of equal volume of protein and reservoir solutions | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Nov 6, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 21589 / % possible obs: 79 % / Observed criterion σ(I): 0 / Redundancy: 2.9 % / Rmerge(I) obs: 0.067 |
Reflection | *PLUS Highest resolution: 1.9 Å / Num. measured all: 61878 |
Reflection shell | *PLUS % possible obs: 44 % / Num. unique obs: 1971 / Num. measured obs: 3897 / Rmerge(I) obs: 0.218 |
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Processing
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Refinement | Resolution: 1.9→8 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 1.9→8 Å
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Refine LS restraints |
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