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Open data
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Basic information
Entry | Database: PDB / ID: 1r3r | ||||||
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Title | Uroporphyrinogen Decarboxylase with mutation D86N | ||||||
![]() | Uroporphyrinogen Decarboxylase | ||||||
![]() | LYASE / uroporphyrinogen decarboxylase coproporphyrinogen / X-ray crystallography | ||||||
Function / homology | ![]() porphyrin-containing compound catabolic process / uroporphyrinogen decarboxylase / uroporphyrinogen decarboxylase activity / porphyrin-containing compound metabolic process / heme B biosynthetic process / heme O biosynthetic process / heme A biosynthetic process / protoporphyrinogen IX biosynthetic process / Heme biosynthesis / heme biosynthetic process ...porphyrin-containing compound catabolic process / uroporphyrinogen decarboxylase / uroporphyrinogen decarboxylase activity / porphyrin-containing compound metabolic process / heme B biosynthetic process / heme O biosynthetic process / heme A biosynthetic process / protoporphyrinogen IX biosynthetic process / Heme biosynthesis / heme biosynthetic process / nucleoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Phillips, J.D. / Whitby, F.G. / Kushner, J.P. / Hill, C.P. | ||||||
![]() | ![]() Title: Structural basis for tetrapyrrole coordination by uroporphyrinogen decarboxylase Authors: Phillips, J.D. / Whitby, F.G. / Kushner, J.P. / Hill, C.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 95 KB | Display | ![]() |
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PDB format | ![]() | 72.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 431.6 KB | Display | ![]() |
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Full document | ![]() | 438.3 KB | Display | |
Data in XML | ![]() | 19.6 KB | Display | |
Data in CIF | ![]() | 29.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1r3qC ![]() 1r3sC ![]() 1r3tC ![]() 1r3vC ![]() 1r3wC ![]() 1r3yC ![]() 1uroS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Details | One URO-D monomer forms the asymmetric unit. URO-D is a dimer in solution and in the crystal. The dimer is formed by the 2-fold crystallographic rotation. |
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Components
#1: Protein | Mass: 40830.781 Da / Num. of mol.: 1 / Mutation: D86N Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.37 Å3/Da / Density % sol: 47.7 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 294 K / Method: liquid diffusion / pH: 6.5 Details: The crystal trial was conducted in an anaerobic chamber, with PBG, PBG-D added to the solution. These conditions are conducive to formation of an enzyme product complex, as the enzyme is ...Details: The crystal trial was conducted in an anaerobic chamber, with PBG, PBG-D added to the solution. These conditions are conducive to formation of an enzyme product complex, as the enzyme is typically active under these conditions (see related strcuture 1R3Q). There is not a ligand bound in this structure. 1.5 M citrate, pH 6.5, LIQUID DIFFUSION, temperature 294K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 21 ℃ / pH: 7.5 / Method: vapor diffusion, sitting drop / Details: Phillips, J.D., (1997) Protein Sci., 6, 1343. | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Jun 15, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→87.71 Å / Num. all: 36928 / Num. obs: 36928 / % possible obs: 96 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5 % / Rmerge(I) obs: 0.083 / Rsym value: 0.083 / Net I/σ(I): 9 |
Reflection shell | Resolution: 1.85→1.92 Å / Redundancy: 5 % / Rmerge(I) obs: 0.437 / Mean I/σ(I) obs: 2.8 / Rsym value: 0.437 / % possible all: 80 |
Reflection | *PLUS Lowest resolution: 20 Å / % possible obs: 96 % / Num. measured all: 175858 |
Reflection shell | *PLUS % possible obs: 79.8 % / Mean I/σ(I) obs: 1.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1URO Resolution: 1.85→87.71 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.95 / SU B: 2.929 / SU ML: 0.083 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.119 / ESU R Free: 0.112 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 20.283 Å2
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Refinement step | Cycle: LAST / Resolution: 1.85→87.71 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.85→1.95 Å / Total num. of bins used: 10 /
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Refinement | *PLUS Lowest resolution: 20 Å / Rfactor Rfree: 0.192 / Rfactor Rwork: 0.161 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 1.85 Å / Lowest resolution: 1.95 Å / Rfactor Rfree: 0.29 |