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Yorodumi- PDB-1qco: CRYSTAL STRUCTURE OF FUMARYLACETOACETATE HYDROLASE COMPLEXED WITH... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1qco | |||||||||
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Title | CRYSTAL STRUCTURE OF FUMARYLACETOACETATE HYDROLASE COMPLEXED WITH FUMARATE AND ACETOACETATE | |||||||||
Components | FUMARYLACETOACETATE HYDROLASE | |||||||||
Keywords | HYDROLASE / MIXED BETA SANDWICH ROLL | |||||||||
Function / homology | Function and homology information homogentisate catabolic process / fumarylacetoacetase / fumarylacetoacetase activity / Tyrosine catabolism / tyrosine catabolic process / L-phenylalanine catabolic process / arginine catabolic process / lipid metabolic process / metal ion binding Similarity search - Function | |||||||||
Biological species | Mus musculus (house mouse) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 1.9 Å | |||||||||
Authors | Timm, D.E. / Mueller, H.A. / Bhanumoorthy, P. / Harp, J.M. / Bunick, G.J. | |||||||||
Citation | Journal: Structure Fold.Des. / Year: 1999 Title: Crystal structure and mechanism of a carbon-carbon bond hydrolase. Authors: Timm, D.E. / Mueller, H.A. / Bhanumoorthy, P. / Harp, J.M. / Bunick, G.J. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qco.cif.gz | 187.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qco.ent.gz | 145.4 KB | Display | PDB format |
PDBx/mmJSON format | 1qco.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qc/1qco ftp://data.pdbj.org/pub/pdb/validation_reports/qc/1qco | 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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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 46440.789 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: PGEX / Production host: Escherichia coli (E. coli) / References: UniProt: P35505, fumarylacetoacetase |
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-Non-polymers , 5 types, 540 molecules
#2: Chemical | #3: Chemical | ChemComp-NI / #4: Chemical | #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.55 Å3/Da / Density % sol: 51.83 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: PEG 6000, SODIUM CACODYLATE, NICKEL ACETATE, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Oct 4, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→27.9 Å / Num. obs: 67124 / % possible obs: 91.4 % / Observed criterion σ(I): 0 / Redundancy: 2.2 % / Biso Wilson estimate: 18.2 Å2 / Rmerge(I) obs: 0.067 / Net I/σ(I): 13.5 |
Reflection shell | Resolution: 1.9→1.97 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.264 / % possible all: 60.9 |
Reflection | *PLUS Num. measured all: 148826 |
Reflection shell | *PLUS % possible obs: 60.9 % |
-Processing
Software |
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Refinement | Resolution: 1.9→27.9 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 1.9→27.9 Å
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Refine LS restraints |
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