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- PDB-1fo6: CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE -
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Open data
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Basic information
Entry | Database: PDB / ID: 1fo6 | ||||||
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Title | CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE | ||||||
![]() | N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE | ||||||
![]() | HYDROLASE / four layer a/b fold | ||||||
Function / homology | ![]() N-carbamoyl-D-amino-acid hydrolase / N-carbamoyl-D-amino acid hydrolase activity / beta-alanine biosynthetic process via 3-ureidopropionate / beta-ureidopropionase activity Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Wang, W.-C. / Hsu, W.-H. / Chien, F.-T. / Chen, C.-Y. | ||||||
![]() | ![]() Title: Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft. Authors: Wang, W.C. / Hsu, W.H. / Chien, F.T. / Chen, C.Y. #1: ![]() Title: Expression, crystallization and preliminary X-ray diffraction studies of N-carbamyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter Authors: Hsu, W.-H. / Chien, F.-T. / Hsu, C.L. / Wang, T.C. / Yuan, H.S. / Wang, W.-C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 257.6 KB | Display | ![]() |
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PDB format | ![]() | 206.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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: 34209.062 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.37 Å3/Da / Density % sol: 48.05 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 296.5 K / Method: vapor diffusion, hanging drop / pH: 7 Details: Lithium sulfate, HEPES , pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 296.5K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 23 ℃ / pH: 7.5 | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||
Radiation wavelength |
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Reflection | Resolution: 1.95→30 Å / Num. all: 93420 / Num. obs: 93415 / % possible obs: 99.9 % / Redundancy: 7.4 % / Rmerge(I) obs: 0.073 / Net I/σ(I): 7.5 | ||||||||||||||||||
Reflection shell | Resolution: 1.95→2 Å / Redundancy: 7.4 % / Rmerge(I) obs: 0.459 / Num. unique all: 6865 / % possible all: 99.9 | ||||||||||||||||||
Reflection | *PLUS Lowest resolution: 30 Å | ||||||||||||||||||
Reflection shell | *PLUS % possible obs: 99.8 % |
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Processing
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Refinement | Resolution: 1.95→30 Å / σ(F): 0 / σ(I): 0 Details: Refinement of Macromolecular Structures by the Maximum-Likelihood Method
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Refinement step | Cycle: LAST / Resolution: 1.95→30 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 30 Å / σ(F): 0 / % reflection Rfree: 5 % / Rfactor Rwork: 0.187 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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