+Open data
-Basic information
Entry | Database: PDB / ID: 1urr | ||||||
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Title | A novel Drosophila Melanogaster Acylphosphatase (AcPDro2) | ||||||
Components | CG18505 PROTEIN | ||||||
Keywords | HYDROLASE / ACYLPHOSPHATASE / ENZYME | ||||||
Function / homology | Function and homology information cellular metabolic process / acylphosphatase / acylphosphatase activity / hydrolase activity / cytoplasm Similarity search - Function | ||||||
Biological species | DROSOPHILA MELANOGASTER (fruit fly) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.5 Å | ||||||
Authors | Rosano, C. / Zuccotti, S. / Bolognesi, M. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2004 Title: Three-Dimensional Structural Characterization of a Novel Drosophila Melanogaster Acylphosphatase Authors: Zuccotti, S. / Rosano, C. / Ramazzotti, M. / Degl'Innocenti, D. / Stefani, M. / Manao, G. / Bolognesi, M. #1: Journal: FEBS Lett. / Year: 2003 Title: Characterization of a Novel Drosophila Melanogaster Acylphosphatase Authors: Degl'Innocenti, D. / Ramazzotti, M. / Marzocchini, R. / Chiti, F. / Raugei, G. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1urr.cif.gz | 58.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1urr.ent.gz | 42.7 KB | Display | PDB format |
PDBx/mmJSON format | 1urr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ur/1urr ftp://data.pdbj.org/pub/pdb/validation_reports/ur/1urr | HTTPS FTP |
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-Related structure data
Related structure data | 2acyS S: Starting model for refinement |
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Similar structure data |
-Links
-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: 11783.540 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) DROSOPHILA MELANOGASTER (fruit fly) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q9VF36, acylphosphatase |
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#2: Chemical | ChemComp-GOL / |
#3: 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: 2.52 Å3/Da / Density % sol: 55.2 % |
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Crystal grow | pH: 4.5 / Details: pH 4.50 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.933 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→39.5 Å / Num. obs: 19859 / % possible obs: 98.7 % / Observed criterion σ(I): 3 / Redundancy: 6.2 % / Biso Wilson estimate: 29.5 Å2 / Rmerge(I) obs: 0.047 / Net I/σ(I): 17.2 |
Reflection shell | Resolution: 1.5→1.55 Å / Rmerge(I) obs: 0.3 / Mean I/σ(I) obs: 2.9 / % possible all: 97.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2ACY Resolution: 1.5→10 Å / SU ML: 0.047 / ESU R Free: 0.079
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Displacement parameters | Biso mean: 26.9 Å2 | ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.5→10 Å
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