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Open data
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Basic information
Entry | Database: PDB / ID: 5k3o | ||||||
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Title | Wolinella succinogenes L-asparaginase P121 and L-Aspartic acid | ||||||
![]() | L-asparaginase | ||||||
![]() | HYDROLASE / L-asparaginase / P121 / L-aspartic acid | ||||||
Function / homology | ![]() asparagine metabolic process / asparaginase / asparaginase activity / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Nguyen, H.A. / Lave, A. | ||||||
![]() | ![]() Title: The differential ability of asparagine and glutamine in promoting the closed/active enzyme conformation rationalizes the Wolinella succinogenes L-asparaginase substrate specificity. Authors: Nguyen, H.A. / Durden, D.L. / Lavie, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 268.7 KB | Display | ![]() |
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PDB format | ![]() | 216.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 464 KB | Display | ![]() |
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Full document | ![]() | 472.6 KB | Display | |
Data in XML | ![]() | 55.7 KB | Display | |
Data in CIF | ![]() | 81.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5k45C ![]() 5k4gC ![]() 5k4hC ![]() 1wsaS 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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2 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: _ / Beg auth comp-ID: LYS / Beg label comp-ID: LYS / End auth comp-ID: TYR / End label comp-ID: TYR / Refine code: _ / Auth seq-ID: 3 - 330 / Label seq-ID: 3 - 330
NCS ensembles :
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Components
#1: Protein | Mass: 34903.742 Da / Num. of mol.: 4 / Mutation: S121P Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W Gene: ansA, ansB, WS0660 / Production host: ![]() ![]() #2: Chemical | ChemComp-ASP / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.33 Å3/Da / Density % sol: 47.12 % |
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Crystal grow | Temperature: 283 K / Method: vapor diffusion, hanging drop / Details: PEG2000, HEPES 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jun 30, 2015 |
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97872 Å / Relative weight: 1 |
Reflection | Resolution: 1.696→30 Å / Num. obs: 139440 / % possible obs: 98.8 % / Redundancy: 3.74 % / Biso Wilson estimate: 21.3 Å2 / Rsym value: 0.065 / Net I/σ(I): 16.37 |
Reflection shell | Resolution: 1.696→1.8 Å / Num. unique all: 22086 / Rsym value: 0.718 / % possible all: 97.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1wsa Resolution: 1.696→30 Å / Cor.coef. Fo:Fc: 0.969 / Cor.coef. Fo:Fc free: 0.954 / SU B: 3.194 / SU ML: 0.094 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.107 / ESU R Free: 0.103 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 99.87 Å2 / Biso mean: 26.87 Å2 / Biso min: 10.09 Å2
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Refinement step | Cycle: final / Resolution: 1.696→30 Å
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Refine LS restraints |
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Refine LS restraints NCS | Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05
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LS refinement shell | Resolution: 1.696→1.74 Å / Total num. of bins used: 20
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