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Open data
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Basic information
Entry | Database: PDB / ID: 1kgg | ||||||
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Title | STRUCTURE OF BETA-LACTAMASE GLU166GLN:ASN170ASP MUTANT | ||||||
![]() | PROTEIN (BETA-LACTAMASE) | ||||||
![]() | HYDROLASE / ANTIBIOTIC RESISTANCE / BETA-LACTAM HYDROLYSIS | ||||||
Function / homology | ![]() beta-lactam antibiotic catabolic process / beta-lactamase / beta-lactamase activity / response to antibiotic Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Chen, C.C.H. / Herzberg, O. | ||||||
![]() | ![]() Title: Relocation of the catalytic carboxylate group in class A beta-lactamase: the structure and function of the mutant enzyme Glu166-->Gln:Asn170-->Asp. Authors: Chen, C.C. / 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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Remark 650 | HELIX SECONDARY STRUCTURE ASSIGNMENT IS ACCORDING TO W. KABSCH AND C. SANDER (BIOPOLYMERS 22, 2577- ...HELIX SECONDARY STRUCTURE ASSIGNMENT IS ACCORDING TO W. KABSCH AND C. SANDER (BIOPOLYMERS 22, 2577-2637, 1983). HELIX NUMBERING IS AS IN 3BLM. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 65.4 KB | Display | ![]() |
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PDB format | ![]() | 47.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 375.9 KB | Display | ![]() |
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Full document | ![]() | 381.8 KB | Display | |
Data in XML | ![]() | 7.3 KB | Display | |
Data in CIF | ![]() | 10.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3blmS 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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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 28974.410 Da / Num. of mol.: 1 / Mutation: E166Q,N170D Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-SO4 / |
#3: Water | ChemComp-HOH / |
Sequence details | RESIDUE NUMBERING IS BASED ON AMBLER, 1979 (R. P. AMBLER, BETA-LACTAMASES, J. M. T. HAMILTON-MILLER ...RESIDUE NUMBERING IS BASED ON AMBLER, 1979 (R. P. AMBLER, BETA-LACTAMASES |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.06 Å3/Da / Density % sol: 65 % | |||||||||||||||||||||||||
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Crystal grow | pH: 8 / Details: pH 8.0 | |||||||||||||||||||||||||
Crystal | *PLUS | |||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: SIEMENS / Detector: AREA DETECTOR |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→20 Å / Num. obs: 15531 / % possible obs: 95.6 % / Observed criterion σ(I): 0 / Redundancy: 3.4 % / Rmerge(I) obs: 0.114 / Net I/σ(I): 11.8 |
Reflection shell | Resolution: 2.3→2.44 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.441 / Mean I/σ(I) obs: 1.8 / % possible all: 87.1 |
Reflection shell | *PLUS % possible obs: 87.1 % / Num. unique obs: 2665 |
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Processing
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Refinement | Method to determine structure: OTHER Starting model: 3BLM Resolution: 2.3→8 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 100000 / Data cutoff low absF: 0 / Cross valid method: THROUGHOUT / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 8 Å / σ(F): 2 / Rfactor obs: 0.178 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 1.9 |