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Open data
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Basic information
Entry | Database: PDB / ID: 4fsk | |||||||||
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Title | Urate oxidase-azide complex in anaerobic conditions | |||||||||
![]() | Uricase | |||||||||
![]() | OXIDOREDUCTASE / INHIBITION / DEGRADATION MECHANISM / PEROXISOME / PURINE METABOLISM / HOMOTETRAMER / OXYGEN BINDING | |||||||||
Function / homology | ![]() purine nucleobase catabolic process / factor-independent urate hydroxylase / urate oxidase activity / urate catabolic process / peroxisome Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Gabison, L. / Colloc'h, N. / El Hajji, M. / Castro, B. / Chiadmi, M. / Prange, T. | |||||||||
![]() | ![]() Title: Azide and Cyanide Have Different Inhibition Modes of Urate Oxidase Authors: Gabison, L. / Colloc'h, N. / El Hajji, M. / Castro, B. / Chiadmi, M. / Prange, T. #1: ![]() Title: Structural Analysis of Urate Oxidase in Complex with its Natural Substrate Inhibited by Cyanide: Mechanistic Implications. Authors: Gabison, L. / Prange, T. / Colloc'h, N. / El Hajji, M. / Castro, B. / Chiadmi, M. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 78.9 KB | Display | ![]() |
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PDB format | ![]() | 56.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 421.6 KB | Display | ![]() |
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Full document | ![]() | 422.9 KB | Display | |
Data in XML | ![]() | 14.5 KB | Display | |
Data in CIF | ![]() | 20.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3p9fS S: Starting model for refinement |
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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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Components
#1: Protein | Mass: 34183.590 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q00511, factor-independent urate hydroxylase | ||||
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#2: Chemical | #3: Chemical | ChemComp-NA / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.81 Å3/Da / Density % sol: 58.36 % |
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Crystal grow | Temperature: 291 K / pH: 10 Details: PROTEIN AT 20 MG/ML IN 50 MM TRIS BUFFER, 0.3 M SODIUM AZIDE, SATURATED WITH URIC ACID, pH 10.0, BATCH METHOD - STTING DROPS, temperature 291K |
-Data collection
Diffraction | Mean temperature: 291 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: May 13, 2009 / Details: BENT MIRROR |
Radiation | Monochromator: SI 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.982 Å / Relative weight: 1 |
Reflection | Resolution: 1.98→38.23 Å / Num. all: 27917 / Num. obs: 26720 / % possible obs: 97.8 % / Observed criterion σ(F): 4 / Observed criterion σ(I): 2 / Redundancy: 4.2 % / Rmerge(I) obs: 0.054 / Net I/σ(I): 3.4 |
Reflection shell | Resolution: 1.98→2.1 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.195 / Mean I/σ(I) obs: 19.5 / % possible all: 93.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 3P9F Resolution: 1.98→38.23 Å / Num. parameters: 10271 / Num. restraintsaints: 9872 / Cross valid method: NONE / σ(F): 0 / σ(I): 2 / Stereochemistry target values: ENGH AND HUBER
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Refine analyze | Num. disordered residues: 7 / Occupancy sum hydrogen: 0 / Occupancy sum non hydrogen: 2545.8 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.98→38.23 Å
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Refine LS restraints |
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