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Open data
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Basic information
Entry | Database: PDB / ID: 8i99 | ||||||
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Title | N-carbamoyl-D-amino-acid hydrolase mutant - M4Th3 | ||||||
![]() | N-carbamoyl-D-amino-acid hydrolase | ||||||
![]() | HYDROLASE / carbon-nitrogen hydrolase / tetramer | ||||||
Function / homology | beta-alanine biosynthetic process via 3-ureidopropionate / beta-ureidopropionase activity / Carbon-nitrogen hydrolase superfamily / Carbon-nitrogen hydrolase / Carbon-nitrogen hydrolase domain profile. / Carbon-nitrogen hydrolase / N-carbamoyl-D-amino-acid hydrolase![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Hu, J.M. / Ni, Y. / Xu, G.C. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Engineering the Thermostability of a d-Carbamoylase Based on Ancestral Sequence Reconstruction for the Efficient Synthesis of d-Tryptophan. Authors: Hu, J. / Chen, X. / Zhang, L. / Zhou, J. / Xu, G. / Ni, Y. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 240.2 KB | Display | ![]() |
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PDB format | ![]() | 194.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 458 KB | Display | ![]() |
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Full document | ![]() | 485.4 KB | Display | |
Data in XML | ![]() | 44.3 KB | Display | |
Data in CIF | ![]() | 60.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | Similarity search - Function & homology ![]() |
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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: 34587.133 Da / Num. of mol.: 4 / Mutation: S202P, E208D, R277L Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: NA8A_19058 / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.93 Å3/Da / Density % sol: 58.08 % |
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Crystal grow | Temperature: 285 K / Method: vapor diffusion, sitting drop / Details: Bis-Tris pH6.5, PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SEALED TUBE / Type: BRUKER D8 QUEST / Wavelength: 1.54178 Å |
Detector | Type: Bruker PHOTON II / Detector: PIXEL / Date: Nov 22, 2022 / Details: multilayer |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 3.17→23.98 Å / Num. obs: 26181 / % possible obs: 98.7 % / Redundancy: 1.9 % / Rmerge(I) obs: 0.128 / Net I/σ(I): 4 |
Reflection shell | Resolution: 3.17→3.39 Å / Rmerge(I) obs: 0.307 / Num. unique obs: 4578 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.17→23.98 Å
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Refine LS restraints |
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LS refinement shell |
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