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Yorodumi- PDB-1bt5: CRYSTAL STRUCTURE OF THE IMIPENEM INHIBITED TEM-1 BETA-LACTAMASE ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1bt5 | ||||||
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Title | CRYSTAL STRUCTURE OF THE IMIPENEM INHIBITED TEM-1 BETA-LACTAMASE FROM ESCHERICHIA COLI | ||||||
Components | PROTEIN (BETA-LACTAMASE) | ||||||
Keywords | HYDROLASE / BETA-LACTAM DEGRADATION | ||||||
Function / homology | Function and homology information beta-lactam antibiotic catabolic process / beta-lactamase activity / beta-lactamase / response to antibiotic Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / OTHER / Resolution: 1.8 Å | ||||||
Authors | Maveyraud, L. / Mourey, L. / Pedelacq, J.D. / Guillet, V. / Kotra, L.K. / Mobashery, S. / Samama, J.P. | ||||||
Citation | Journal: J.Am.Chem.Soc. / Year: 1998 Title: Structural Basis for Clinical Longevity of Carbapenem Antibiotics in the Face of Challenge by the Common Class A Beta-Lactamases from Antibiotic-Resistant Bacteria Authors: Maveyraud, L. / Mourey, L. / Kotra, L.P. / Pedelacq, J.D. / Guillet, V. / Mobashery, S. / Samama, J.P. #1: Journal: Proteins / Year: 1993 Title: Crystal Structure of Escherichia Coli Tem1 Beta-Lactamase at 1.8 A Resolution Authors: Jelsch, C. / Mourey, L. / Masson, J.M. / Samama, J.P. #2: Journal: J.Mol.Biol. / Year: 1992 Title: Crystallization and Preliminary Crystallographic Data on Escherichia Coli Tem1 Beta-Lactamase Authors: Jelsch, C. / Lenfant, F. / Masson, J.M. / Samama, J.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bt5.cif.gz | 75.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bt5.ent.gz | 55.3 KB | Display | PDB format |
PDBx/mmJSON format | 1bt5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1bt5_validation.pdf.gz | 732.1 KB | Display | wwPDB validaton report |
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Full document | 1bt5_full_validation.pdf.gz | 733.1 KB | Display | |
Data in XML | 1bt5_validation.xml.gz | 15.9 KB | Display | |
Data in CIF | 1bt5_validation.cif.gz | 24.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bt/1bt5 ftp://data.pdbj.org/pub/pdb/validation_reports/bt/1bt5 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 28984.076 Da / Num. of mol.: 1 / Mutation: V82I, A182V Source method: isolated from a genetically manipulated source Details: ESTER LINK BETWEEN SER A 70 OG AND IM2 350 C7 / Source: (gene. exp.) Escherichia coli (E. coli) / Cellular location: PERIPLASMIC / Gene: BLA / Variant: V82I, A182V / Cellular location (production host): PERIPLASM / Production host: Escherichia coli (E. coli) / References: UniProt: P62593, beta-lactamase | ||||
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#2: Chemical | ChemComp-SO4 / #3: Chemical | ChemComp-IM2 / ( | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.94 Å3/Da / Density % sol: 36.2 % |
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Crystal grow | pH: 7.8 / Details: pH 7.8 |
Crystal grow | *PLUS Method: other / Details: Jelsch, C., (1992) J. Mol. Biol., 223, 377. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X31 / Wavelength: 1.1271 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 15, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1271 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→18 Å / Num. obs: 21770 / % possible obs: 98.3 % / Observed criterion σ(I): 0 / Redundancy: 3.9 % / Biso Wilson estimate: 12.13 Å2 / Rsym value: 0.059 / Net I/σ(I): 20.9 |
Reflection shell | Resolution: 1.8→1.89 Å / Redundancy: 3.6 % / Mean I/σ(I) obs: 8.7 / Rsym value: 0.116 / % possible all: 96.8 |
Reflection | *PLUS Num. measured all: 84646 / Rmerge(I) obs: 0.059 |
Reflection shell | *PLUS % possible obs: 96.8 % / Rmerge(I) obs: 0.116 |
-Processing
Software |
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Refinement | Method to determine structure: OTHER / Resolution: 1.8→18 Å / Cross valid method: THROUGHOUT / σ(F): 0 Details: EXTERNAL BULK SOLVENT CORRECTION COMPUTED WITH XPLOR 3.1
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Displacement parameters | Biso mean: 10.73 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→18 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS % reflection Rfree: 5 % / Rfactor obs: 0.173 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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