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- PDB-1w61: proline racemase in complex with 2 molecules of pyrrole-2-carboxy... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1w61 | ||||||
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Title | proline racemase in complex with 2 molecules of pyrrole-2-carboxylic acid (holo form) | ||||||
![]() | B-CELL MITOGEN | ||||||
![]() | RACEMASE / RACEMASE PYRIDOXAL PHOSPHATE-INDEPENDENT / STEREO INVERSION / B-CELL MITOGEN / ACID/BASE CATALYSIS / HOMODIMER / ALPHA/BETA DOMAINS | ||||||
Function / homology | ![]() proline racemase activity / proline racemase / 4-hydroxyproline epimerase activity / multicellular organism development / extracellular region / membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Buschiazzo, A. / Alzari, P. | ||||||
![]() | ![]() Title: Crystal Structure,Catalytic Mechanism and Mitogenic Properties of Trypanosoma Cruzi Proline Racemase Authors: Buschiazzo, A. / Goytia, M. / Shaeffer, F. / Degrave, W. / Shepard, W. / Gregoire, C. / Chamond, N. / Cosson, A. / Berneman, A. / Coatnoan, N. / Alzari, P. / Minoprio, P. | ||||||
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. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 152.1 KB | Display | ![]() |
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PDB format | ![]() | 120 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 450.7 KB | Display | ![]() |
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Full document | ![]() | 458.7 KB | Display | |
Data in XML | ![]() | 30 KB | Display | |
Data in CIF | ![]() | 43.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.4124, 0.2854, 0.8651), Vector: |
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Components
#1: Protein | Mass: 45796.246 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q9NCP4, UniProt: Q4DA80*PLUS, proline racemase #2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | THE FIRST 31 AA IN Q9NCP4 CONSTITUTE A SIGNAL PEPTIDE AND THEY WERE REMOVED IN THE CONSTRUCTION ...THE FIRST 31 AA IN Q9NCP4 CONSTITUTE | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50.8 % Description: THE INITIAL MODEL WAS OBTAINED USING ANOMALOUS DIFFRACTION ON SE-MET SUBSTITUTED CRYSTALS. THE REFINEMENT OF THIS INITIAL MODEL WAS NOT COMPLETED -RES 3 ANGSTROMS- BUT USED SUCCESFULLY ...Description: THE INITIAL MODEL WAS OBTAINED USING ANOMALOUS DIFFRACTION ON SE-MET SUBSTITUTED CRYSTALS. THE REFINEMENT OF THIS INITIAL MODEL WAS NOT COMPLETED -RES 3 ANGSTROMS- BUT USED SUCCESFULLY AS MOLECULAR REPLACEMENT PROBE |
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Crystal grow | pH: 5.6 Details: 15% PEG 4000,100MM NH4ACETATE 50MM NA3CITRATE.2H2O,PH5.6, pH 5.60 |
-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Details: TOROIDAL MIRROR |
Radiation | Monochromator: SI(111) CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0072 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→69.2 Å / Num. obs: 46967 / % possible obs: 98.8 % / Observed criterion σ(I): 2 / Redundancy: 3.7 % / Biso Wilson estimate: 23.92 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 15.4 |
Reflection shell | Resolution: 2.1→2.21 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.13 / Mean I/σ(I) obs: 7.7 / % possible all: 94.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: MODEL OF THE SAME PROTEIN OBTAINED BY SAD Resolution: 2.1→30 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.942 / SU B: 6.436 / SU ML: 0.093 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.164 / ESU R Free: 0.149 / 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: 1.2 Å / Solvent model: MASK BULK SOLVENT | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 22.6 Å2
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Refinement step | Cycle: LAST / Resolution: 2.1→30 Å
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Refine LS restraints |
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