+Open data
-Basic information
Entry | Database: PDB / ID: 1bmc | ||||||
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Title | STRUCTURE OF A ZINC METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS | ||||||
Components | METALLO-BETA-LACTAMASE | ||||||
Keywords | HYDROLASE (ACTING IN CYCLIC AMIDES) / ANTIBIOTIC RESISTANCE | ||||||
Function / homology | Function and homology information antibiotic catabolic process / beta-lactamase activity / beta-lactamase / periplasmic space / response to antibiotic / zinc ion binding Similarity search - Function | ||||||
Biological species | Bacillus cereus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | ||||||
Authors | Carfi, A. / Pares, S. / Duee, E. / Dideberg, O. | ||||||
Citation | Journal: EMBO J. / Year: 1995 Title: The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. Authors: Carfi, A. / Pares, S. / Duee, E. / Galleni, M. / Duez, C. / Frere, J.M. / Dideberg, O. #1: Journal: Biochem.J. / Year: 1987 Title: An X-Ray-Crystallographic Study of Beta-Lactamase II from Bacillus Cereus at 0.35 Nm Resolution Authors: Sutton, B.J. / Artymiuk, P.J. / Cordero-Borboa, A.E. / Little, C. / Phillips, D.C. / Waley, S.G. #2: Journal: FEBS Lett. / Year: 1985 Title: The Amino Acid Sequence of the Zinc-Requiring Beta-Lactamase II from the Bacterium Bacillus Cereus 569 Authors: Ambler, R.P. / Daniel, M. / Fleming, J. / Hermoso, J.M. / Pang, C. / Waley, S.G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bmc.cif.gz | 50 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bmc.ent.gz | 36 KB | Display | PDB format |
PDBx/mmJSON format | 1bmc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bm/1bmc ftp://data.pdbj.org/pub/pdb/validation_reports/bm/1bmc | HTTPS FTP |
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-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: 24293.723 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus cereus (bacteria) / Strain: 569-H / References: UniProt: P04190, beta-lactamase |
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#2: Chemical | ChemComp-ZN / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.33 Å3/Da / Density % sol: 37.7 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
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Detector | Type: ENRAF-NONIUS FAST / Detector: DIFFRACTOMETER / Date: Jul 1, 1994 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→25 Å / Num. obs: 6911 / % possible obs: 86 % / Observed criterion σ(I): 0 / Redundancy: 2 % / Rmerge(I) obs: 0.03 |
Reflection | *PLUS Num. measured all: 11206 / Rmerge(I) obs: 0.03 |
-Processing
Software |
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Refinement | Resolution: 2.5→8 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 1.47 |