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Yorodumi- PDB-1fxh: MUTANT OF PENICILLIN ACYLASE IMPAIRED IN CATALYSIS WITH PHENYLACE... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fxh | ||||||
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Title | MUTANT OF PENICILLIN ACYLASE IMPAIRED IN CATALYSIS WITH PHENYLACETIC ACID IN THE ACTIVE SITE | ||||||
Components | (PENICILLIN ACYLASEPenicillin amidase) x 2 | ||||||
Keywords | HYDROLASE / Ntn-hydrolase fold | ||||||
Function / homology | Function and homology information penicillin amidase / penicillin amidase activity / antibiotic biosynthetic process / periplasmic space / response to antibiotic / metal ion binding Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.97 Å | ||||||
Authors | Alkema, W.B. / Hensgens, C.M. / Kroezinga, E.H. / de Vries, E. / Floris, R. / van der Laan, J.M. / Dijkstra, B.W. / Janssen, D.B. | ||||||
Citation | Journal: Protein Eng. / Year: 2000 Title: Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and site-directed mutagenesis studies. Authors: Alkema, W.B. / Hensgens, C.M. / Kroezinga, E.H. / de Vries, E. / Floris, R. / van der Laan, J.M. / Dijkstra, B.W. / Janssen, D.B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fxh.cif.gz | 178.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fxh.ent.gz | 137 KB | Display | PDB format |
PDBx/mmJSON format | 1fxh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fx/1fxh ftp://data.pdbj.org/pub/pdb/validation_reports/fx/1fxh | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The biological assembly is a hetero dimer. |
-Components
#1: Protein | Mass: 23838.824 Da / Num. of mol.: 1 / Fragment: ALPHA SUBUNIT Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PEC / Production host: Escherichia coli (E. coli) / References: UniProt: P06875, penicillin amidase |
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#2: Protein | Mass: 62400.496 Da / Num. of mol.: 1 / Fragment: BETA SUBUNIT / Mutation: N241A, V148L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PEC / Production host: Escherichia coli (E. coli) / References: UniProt: P06875, penicillin amidase |
#3: Chemical | ChemComp-CA / |
#4: Chemical | ChemComp-PAC / |
#5: 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: 2.18 Å3/Da / Density % sol: 43.59 % | ||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.2 Details: PEG MME 2000, MOPS, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃Details: drop consists of equal amounts of protein and precipitant solutions | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X31 / Wavelength: 1.04 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 25, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.04 Å / Relative weight: 1 |
Reflection | Resolution: 1.97→20 Å / Num. all: 51862 / Num. obs: 50404 / % possible obs: 97.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 1.8 % / Biso Wilson estimate: 5.7 Å2 / Rmerge(I) obs: 0.041 / Net I/σ(I): 15.7 |
Reflection shell | Resolution: 1.97→2 Å / Rmerge(I) obs: 0.124 / Num. unique all: 0 / % possible all: 95 |
Reflection shell | *PLUS % possible obs: 95 % |
-Processing
Software |
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Refinement | Resolution: 1.97→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: ENGH & HUBER / Details: USED MAXIMUM LIKELYHOOD
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Refinement step | Cycle: LAST / Resolution: 1.97→20 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Classification: refinement | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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