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- PDB-1war: Recombinant Human Purple Acid Phosphatase expressed in Pichia Pastoris -
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Open data
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Basic information
Entry | Database: PDB / ID: 1war | ||||||
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Title | Recombinant Human Purple Acid Phosphatase expressed in Pichia Pastoris | ||||||
![]() | HUMAN PURPLE ACID PHOSPHATASE | ||||||
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Function / homology | ![]() negative regulation of superoxide anion generation / Vitamin B2 (riboflavin) metabolism / riboflavin metabolic process / negative regulation of macrophage cytokine production / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Duff, A.P. / Langley, D.B. / Han, R. / Averill, B.A. / Freeman, H.C. / Guss, J.M. | ||||||
![]() | ![]() Title: Crystal Structures of Recombinant Human Purple Acid Phosphatase with and without an Inhibitory Conformation of the Repression Loop. Authors: Strater, N. / Jasper, B. / Scholte, M. / Krebs, B. / Duff, A.P. / Langley, D.B. / Han, R. / Averill, B.A. / Freeman, H.C. / Guss, J.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 | ![]() | 127.1 KB | Display | ![]() |
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PDB format | ![]() | 99.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2bq8C ![]() 1uteS C: citing same article ( 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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Unit cell |
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Components
#1: Protein | Mass: 35053.641 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: A SIX AMINO ACID CLONING ARTIFACT IS ATTACHED TO THE N-TERMINUS Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q6IAS6, UniProt: P13686*PLUS, ![]() | ||||||||
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#2: Chemical | ![]() #3: Chemical | ChemComp-PO4 / | ![]() #4: Sugar | ChemComp-NAG / | ![]() #5: Water | ChemComp-HOH / | ![]() Sequence details | THE FIRST 20 RESIDUES OF Q6IAS6 ARE NOT PART OF THE MATURE ENZYME. THE MATURE PROTEIN COMPRISES ...THE FIRST 20 RESIDUES OF Q6IAS6 ARE NOT PART OF THE MATURE ENZYME. THE MATURE PROTEIN COMPRISES RESIDUES 21-325 AS NUMBERED IN Q6IAS6. A SIX AMINO ACID CLONING ARTIFACT IS ATTACHED TO THE N-TERMINUS OF THE MATURE PROTEIN. | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.91 Å3/Da / Density % sol: 57.7 % |
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Crystal grow![]() | Temperature: 277 K Details: THE PROTEIN (10 MG/ML) IN 50 MM MES AT PH 6, WAS PASSED THROUGH AN ULTRAFREE-MC 0.22 MM SPIN FILTER UNIT (MILLIPORE) AND ALLOWED TO STAND AT 4 DEGREES C. PURPLE CRYSTALS GREW SPONTANEOUSLY ...Details: THE PROTEIN (10 MG/ML) IN 50 MM MES AT PH 6, WAS PASSED THROUGH AN ULTRAFREE-MC 0.22 MM SPIN FILTER UNIT (MILLIPORE) AND ALLOWED TO STAND AT 4 DEGREES C. PURPLE CRYSTALS GREW SPONTANEOUSLY OVERNIGHT AND REACHED SIZES UP TO 0.5 MM IN SEVERAL WEEKS. |
-Data collection
Diffraction | Mean temperature: 300 K |
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Diffraction source | Source: ![]() |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Aug 20, 2003 / Details: OSMIC MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.22→18.98 Å / Num. obs: 15951 / % possible obs: 94.5 % / Observed criterion σ(I): -3 / Redundancy: 4.2 % / Biso Wilson estimate: 36 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 17.97 |
Reflection shell | Resolution: 2.22→2.3 Å / Redundancy: 4.2 % / Rmerge(I) obs: 0.4 / Mean I/σ(I) obs: 5.49 / % possible all: 94 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 1UTE Resolution: 2.22→18.98 Å / Cor.coef. Fo:Fc: 0.975 / Cor.coef. Fo:Fc free: 0.95 / SU B: 5.02 / SU ML: 0.126 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.23 / ESU R Free: 0.187 / 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: 32.02 Å2
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Refinement step | Cycle: LAST / Resolution: 2.22→18.98 Å
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Refine LS restraints |
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